ID	1.1.1.1
********************************************************************************
*                                                                              *
* Copyrighted by Dietmar Schomburg, Techn. University Braunschweig, GERMANY    *
* Distributed under the License as stated at http:/www.brenda-enzymes.org      *
*                                                                              *
********************************************************************************

PROTEIN
PR	#1# Gallus gallus   <44>
PR	#2# Cricetulus griseus   <1>
PR	#3# Vicia faba   <4>
PR	#4# Drosophila melanogaster   <8,43,58,62,63,64,65>
PR	#5# Mus musculus   <9,48,117,119,141,142,200,212>
PR	#6# Thermus thermophilus   <169,269>
PR	#7# Escherichia coli   <135>
PR	#8# Homo sapiens
	<10,11,12,13,14,15,16,17,18,19,20,21,22,23,53,96,107,109,115,116,119
	124,150,180,186,191,194,206,228,229,273>
PR	#9# Rattus norvegicus   <10,49,50,51,142,167,224,228>
PR	#10# Saccharomyces cerevisiae
	<3,86,87,88,89,90,91,94,104,120,121,122,139,144,148,179,182,184,187,189
	190,192,196,199,202,203,247,251,261,270,278,282,285>
PR	#11# Triticum aestivum   <80>
PR	#12# Oryctolagus cuniculus   <45,46>
PR	#13# Geobacillus stearothermophilus   <126,234,269>
PR	#14# Aspergillus nidulans   <81>
PR	#15# Neurospora crassa   <134,172>
PR	#16# Hordeum vulgare   (#16# isoenzyme mMDH <79>) <79>
PR	#17# Pisum sativum   <80>
PR	#18# Zea mays   <75,76,80,97>
PR	#19# Glycine max   <71,80>
PR	#20# Arabidopsis thaliana   <284>
PR	#21# Petroselinum crispum   <72>
PR	#22# Avena sativa   <80>
PR	#23# Entamoeba histolytica   <100,123,128>
PR	#24# Pseudomonas fluorescens   <106>
PR	#25# Devosia riboflavina   <188>
PR	#26# Pseudomonas aeruginosa   <129,135>
PR	#27# Brassica napus   <74>
PR	#28# Acinetobacter calcoaceticus   <133>
PR	#29# Haloferax volcanii   <240>
PR	#30# Natronomonas pharaonis   <181>
PR	#31# Camellia sinensis   <73>
PR	#32# Schizosaccharomyces pombe   <91>
PR	#33# Klebsiella pneumoniae   <135>
PR	#34# Corynebacterium glutamicum   <242>
PR	#35# Mesocricetus auratus   <47,95>
PR	#36# Micrococcus luteus   <248>
PR	#37# Meyerozyma guilliermondii   <85>
PR	#38# Kluyveromyces marxianus   <3>
PR	#39# Rhodococcus erythropolis   <131>
PR	#40# Equus caballus
	<26,27,28,29,30,31,32,33,34,35,36,37,39,40,41,42,54,55,86,92,93,98,102
	116,117,143,178,198,201,204,275,277>
PR	#41# Zymomonas mobilis   <67,68,140,263>
PR	#42# Macaca mulatta   <25>
PR	#43# Rhodococcus ruber   <114,232>
PR	#44# Oryza sativa   <6,80>
PR	#45# Sulfolobus solfataricus
	<56,66,70,152,153,154,155,158,159,160,163,164,165>
PR	#46# Brevibacterium sp.   <149>
PR	#47# Oenococcus oeni   <223>
PR	#48# Thermus sp.   <166>
PR	#49# Hafnia alvei   <135>
PR	#50# Citrobacter sp.   <279>
PR	#51# Candida sp.   <82>
PR	#52# Oncorhynchus mykiss   <59>
PR	#53# Cucumis melo   <151>
PR	#54# Desulfovibrio gigas   <99>
PR	#55# Thermotoga maritima   <255>
PR	#56# Methylobacterium extorquens   <147>
PR	#57# Fragaria x ananassa   <147>
PR	#58# Suncus murinus   <5>
PR	#59# Malus domestica   <146>
PR	#60# Acetobacter pasteurianus   <113>
PR	#61# Kluyveromyces lactis   <145>
PR	#62# Naja naja   <57>
PR	#63# Citrullus lanatus   <80>
PR	#64# Vitis vinifera   <183>
PR	#65# Klebsiella oxytoca   <135>
PR	#66# Triticum monococcum   <78>
PR	#67# Chlamydomonas moewusii   <69>
PR	#68# Coturnix coturnix   <60>
PR	#69# Sporotrichum pulverulentum   <84>
PR	#70# Thermoanaerobacter brockii   <103,121,205>
PR	#71# Drosophila virilis   <8,64>
PR	#72# Ctenopharyngodon idella   <2>
PR	#73# Najas marina   <7>
PR	#74# Drosophila simulans   <8,63,64>
PR	#75# Drosophila funebris   <8>
PR	#76# Drosophila immigrans   <8>
PR	#77# Scaptodrosophila lebanonensis   <8,38,61,130>
PR	#78# Saimiri sciureus   <24>
PR	#79# Saara hardwickii   <52>
PR	#80# Triticum turgidum   (#80# isoenzyme mMDH <77>) <77>
PR	#81# Euglena longa   <83>
PR	#82# Alligator mississippiensis   <101>
PR	#83# Pelophylax perezi   <125>
PR	#84# Carboxydothermus hydrogenoformans   <226>
PR	#85# Mucor circinelloides   <136>
PR	#86# Aeropyrum pernix   <127,238>
PR	#87# Thermomicrobium roseum   <118>
PR	#88# Zygosaccharomyces rouxii   <132>
PR	#89# Crocus sativus   <105>
PR	#90# Anastrepha fraterculus   <208>
PR	#91# Flavobacterium frigidimaris Q8L3C9 SwissProt <144>
PR	#92# Leifsonia sp.   <137>
PR	#93# Sulfolobus solfataricus Q9UXF1 UniProt (#93# ODC1 <162>) <162>
PR	#94# Sulfolobus sp. P50381 UniProt <159>
PR	#95# Pseudomonas putida Q76HN6 UniProt <156>
PR	#96# Candida parapsilosis B2KJ46 UniProt <168>
PR	#97# Neurospora crassa Q9P6C8 SwissProt <172>
PR	#98# Picrophilus torridus Q6L0S1 SwissProt <173>
PR	#99# Corynebacterium glutamicum R   <171>
PR	#100# Dipodascus capitatus   <185>
PR	#101# Schizosaccharomyces pombe Q09669 SwissProt <174>
PR	#102# Kluyveromyces marxianus A1IIA3 SwissProt <177>
PR	#102# Kluyveromyces marxianus A1IIA3 UniProt <177>
PR	#103# Kluyveromyces marxianus A1IIA4 SwissProt <177>
PR	#103# Kluyveromyces marxianus A1IIA4 UniProt <177>
PR	#104# Sulfolobus solfataricus P39462  <108,157,161,207,216,220,221,235>
PR	#104# Sulfolobus solfataricus P39462 SwissProt
	<108,157,161,207,216,220,221,235>
PR	#104# Sulfolobus solfataricus P39462 UniProt
	<108,157,161,207,216,220,221,235>
PR	#105# Homo sapiens P00326 UniProt <214>
PR	#106# Thermoanaerobacter ethanolicus Q0PH30 UniProt <195>
PR	#107# Anastrepha obliqua   <208>
PR	#108# Homo sapiens P08319 UniProt <214>
PR	#109# Parageobacillus thermoglucosidans Q6RS93 UniProt <210>
PR	#110# Thermoplasma acidophilum Q9HIM3 UniProt <213>
PR	#111# Thermus sp. B2ZRE3 UniProt <197>
PR	#112# Saccharomyces carlsbergensis B6UQD0 UniProt <202>
PR	#113# Geobacillus thermodenitrificans A4IP64 UniProt <215>
PR	#114# Geobacillus thermodenitrificans A4ISB9 UniProt <215>
PR	#115# Mus musculus Q9QYY9  <110>
PR	#116# Saccharomyces cerevisiae P00330  <193,205,209>
PR	#117# Equus caballus P00327  <111,175,205>
PR	#118# Geobacillus stearothermophilus P42328
	<112,176,246,256,257,258,260>
PR	#118# Geobacillus stearothermophilus P42328 UniProt
	<112,176,246,256,257,258,260>
PR	#119# Saccharomyces cerevisiae P00331  <170>
PR	#120# Euglena gracilis B8QU18  (#120# At5g56760, SERAT1.1 <211>) <211>
PR	#121# Sulfolobus tokodaii F9VMI9 SwissProt <217>
PR	#122# Sulfolobus acidocaldarius Q4J702 UniProt <219>
PR	#123# Sulfolobus acidocaldarius Q4J9F2 UniProt <218,219>
PR	#124# Glycine max Q9ZT38 UniProt <233>
PR	#125# Bombyx mori Q1G151 UniProt <231>
PR	#126# Ogataea angusta H9ZGN0 UniProt <222>
PR	#127# Candida maris   <225>
PR	#128# Pyrococcus furiosus Q8U259 SwissProt <230>
PR	#129# Columba livia P86883 UniProt <227>
PR	#130# Scyliorhinus canicula P86884 UniProt <227>
PR	#131# Aeropyrum pernix Q9Y9P9 UniProt <127,236,239>
PR	#132# Haloferax volcanii D4GSN2 UniProt <237>
PR	#133# Thermoanaerobacter pseudethanolicus B0KBL1 UniProt <249>
PR	#134# Thermoanaerobacter pseudethanolicus B0KBJ9 UniProt <249>
PR	#135# Kluyveromyces marxianus G3FFC9 UniProt <252>
PR	#136# Kluyveromyces marxianus V9SDP6 UniProt <252>
PR	#137# Kluyveromyces marxianus V9SCJ1 UniProt <252>
PR	#138# Kluyveromyces marxianus V9SFA1 UniProt <252>
PR	#139# Sulfolobus tokodaii Q96XE0 UniProt <254>
PR	#140# Zymomonas mobilis subsp. mobilis P0DJA2 UniProt <253>
PR	#141# Moraxella sp. P81786 UniProt <260>
PR	#142# Pyrococcus furiosus Q8TZM9 UniProt <138,268>
PR	#143# Ruminiclostridium thermocellum A3DCI2 UniProt <259,264,265,267>
PR	#144# Lactococcus lactis subsp. lactis Q9CEN0 UniProt <250>
PR	#145# Streptococcus thermophilus Q5M4K4 UniProt <262>
PR	#146# Thermoanaerobacterium saccharolyticum I3VSF1 UniProt <259>
PR	#147# Thermoanaerobacter sp. B0K3U7 UniProt <266>
PR	#148# Parageobacillus thermoglucosidans A0A0J9X1L6 UniProt <241>
PR	#149# Thermococcus kodakarensis Q5JI09 UniProt <243>
PR	#150# Yokenella sp. W6CX26 UniProt <244>
PR	#151# Thermoanaerobacter sp. B0K4A2 UniProt <245>
PR	#152# Kangiella koreensis C7R702 UniProt <272>
PR	#153# Rhodococcus ruber Q8KLT9 UniProt <280>
PR	#154# Mycobacterium sp. W8VSK8 UniProt <271>
PR	#155# Thermoanaerobacter sp. X514 B0K4A2 UniProt <281>
PR	#156# Thermoanaerobacter ethanolicus C7IV28 UniProt <281>
PR	#157# Polytomella sp. Pringsheim 198.80 Q70YJ9 UniProt <283>
PR	#158# Blastobotrys adeninivorans A0A060TBM3 UniProt <276>
PR	#159# Parvibaculum lavamentivorans   <274>

RECOMMENDED_NAME
RN	alcohol dehydrogenase


SYSTEMATIC_NAME
SN	alcohol:NAD+ oxidoreductase


SYNONYMS
SY	 aldehyde reductase
SY	 dehydrogenase, alcohol
SY	 alcohol dehydrogenase (NAD)
SY	 aliphatic alcohol dehydrogenase
SY	 ethanol dehydrogenase
SY	 NAD-specific aromatic alcohol dehydrogenase
SY	 NADH-alcohol dehydrogenase
SY	 NADH-aldehyde dehydrogenase
SY	 primary alcohol dehydrogenase
SY	 yeast alcohol dehydrogenase
SY	 FDH
SY	 FALDH
SY	 40 kDa allergen
SY	 ADH-A2
SY	 ADH-B2
SY	 ADH-C2
SY	 ADH-HT
SY	 Alcohol dehydrogenase-B2
SY	 Gastric alcohol dehydrogenase
SY	 Glutathione-dependent formaldehyde dehydrogenase
SY	 GSH-FDH
SY	 Octanol dehydrogenase
SY	 Retinol dehydrogenase
SY	 medium-chain NAD+-dependent ADH <211>
SY	 NAD+-ADH <211>
SY	#10# SCAD <182>
SY	#10# YADH <120,121,179>
SY	#10# Y-ADH <122>
SY	#10# alcohol dehydrogenase I <104,199>
SY	#10# YADH-1 <189>
SY	#10# Adh1p <190>
SY	#10# ADH I <247>
SY	#10# alcohol:NAD+ oxidoreductase <199>
SY	#10# YLL056C <285>
SY	#10,41# alcohol dehydrogenase II <140,170>
SY	#102# KmADH3 <177>
SY	#103# KmADH4 <177>
SY	#104# NAD+-dependent (S)-stereospecific alcohol dehydrogenase <207>
SY	#104# ADH-10 <235>
SY	#104# alcohol dehydrogenase 10 <235>
SY	#104# SsADH-10 <235>
SY	#104# SSO2536 (#104# locus name <235>) <235>
SY	#105# ADH1C (#105# isozyme <214>) <214>
SY	#106# aldehyde/alcohol dehydrogenase <195>
SY	#106,134,143,146,151,155,156,157# AdhE (#106# the purified AdhE
	exhibits high enzymatic activity attributed to aldehyde dehydrogenase
	and low alcohol dehydrogenase activity <195>; #143,146# bifunctional
	alcohol and aldehyde dehydrogenase gene <259>; #151# bifunctional
	enzyme, catalyzes reactions of EC 1.1.1.1 and EC 1.2.1.10 <245>; #134#
	bifunctional secondary ADH/aldehyde hydrogenase <249>; #155,156,157#
	bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol
	dehydrogenase activities <281,283>) <195,245,249,259,265,267,281,283>
SY	#109# ADH-I <210>
SY	#110# Ta1316 ADH <213>
SY	#113,114# long-chain alkyl alcohol dehydrogenase <215>
SY	#121# ST0053 <217>
SY	#121# NAD-dependent medium-chain ADH <217>
SY	#122# SaADH <219>
SY	#122# short-chain ADH <219>
SY	#122# short-chain NAD(H)-dependent dehydrogenase/reductase <219>
SY	#123# SaADH2 <218>
SY	#123# Saci_1232 (#123# gene name <219>) <219>
SY	#126# HpADH3 <222>
SY	#127# NADH-dependent alcohol dehydrogenase <225>
SY	#127# AFPDH <225>
SY	#127# (R)-specific alcohol dehydrogenase <225>
SY	#128# AdhC <230>
SY	#128# PF0991 protein <230>
SY	#129# class I ALDH <227>
SY	#13# HtADH <176>
SY	#130# ADH class III <227>
SY	#131# APE2239 <239>
SY	#131# APE_2239.1 (#131# locus name <236>) <236>
SY	#132# HvADH1 <237>
SY	#132# HVO_2428 (#132# locus name <237>) <237>
SY	#133# Teth39_0218 (#133# gene name <249>) <249>
SY	#133,140,145# AdhB (#133# bifunctional secondary ADH/Acetyl-CoA
	thioesterase <249>) <249,253,262>
SY	#134# Teth39_0206 (#134# gene name <249>) <249>
SY	#139# NAD-dependent alcohol dehydrogenase <254>
SY	#140# alcohol dehydrogenase 2 <253>
SY	#142# AdhD <138,268>
SY	#142# PF1960 (#142# gene name <138>) <138>
SY	#143# Cthe_0423 (#143# gene name <265,267>) <265,267>
SY	#146# Tsac_0416 (#146# gene name <259>) <259>
SY	#147# iron-containing alcohol dehydrogenase <266>
SY	#148# bifunctional alcohol/aldehyde dehydrogenase (#148# catalyzes
	reactions of EC 1.1.1.1 and EC 1.2.1.10 <241>) <241>
SY	#149# TK0845 (#149# gene name <243>) <243>
SY	#151# Teth514_0627 (#151# gene name <245>) <245>
SY	#153# SADH <280>
SY	#153# ADH-A <280>
SY	#154# ADS1 <271>
SY	#158# Aadh1 <276>
SY	#158# ARAD1B16786p <276>
SY	#34,98,144# AdhA <173,242,250>
SY	#40# HLAD <204>
SY	#41# ADH II <140>
SY	#43# sec-ADH A <114>
SY	#43# medium-chain secondary alcohol dehydrogenase <114>
SY	#43# ADH6Hp <232>
SY	#45# alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent (#45# the
	enzyme transfers the pro-R hydrogen from coenzyme to substrate and is
	therefore an A-specific dehydrogenase <155>) <155>
SY	#45,104# SSADH <165,220,221>
SY	#47# NAD+-dependent alcohol dehydrogenase <223>
SY	#48# TaDH <166>
SY	#5# class III alcohol dehydrogenase <141>
SY	#5# alcohol dependent dehydrogenase <200>
SY	#5# ADH 1 <212>
SY	#5,10,23,29,93,105,114,124,136# ADH2 (#10,105# isozyme <202,214>)
	<110,123,128,162,170,202,214,215,233,240,252>
SY	#5,126# alcohol dehydrogenase 3 <200,222>
SY	#5,15,41,102,105,137# ADH3 (#105# isozyme <214>)
	<141,172,177,200,214,252,263>
SY	#5,8,10# alcohol dehydrogenase 1 (#10# mutant enzyme S109P/L116S/Y294C
	<193>) <190,193,212,228>
SY	#5,8,10,13,26,36,40,45,60,70,86,87,90,94,104,107,110,111,124,125# ADH
	<108,111,113,115,117,118,119,126,127,129,152,153,154,155,157,158,159
	160,161,163,164,194,196,197,199,200,201,203,205,206,207,208,209,211,213
	229,231,233,248,251,261>
SY	#53# Cm-ADH2 <151>
SY	#6# NAD(H)-dependent alcohol dehydrogenase <169>
SY	#61# KlDH3 <145>
SY	#61# KlADH4 <145>
SY	#70# TBADH <121>
SY	#77# DADH <130>
SY	#8# ALDH <229>
SY	#8# ADH1C*1 <116>
SY	#8# ADH1C*2 <116>
SY	#8# aldehyde dehydrogenase <229>
SY	#8# class III ADH <229>
SY	#8# class I ADH (#8# isoenzyme <206>; #8# isozyme <180>) <180,206,229>
SY	#8# class II ADH (#8# isoenzyme <206>; #8# isozyme <180>) <180,206,229>
SY	#8# class IV ADH (#8# isozyme <180>) <180,229>
SY	#8# ADH1B <273>
SY	#8,10,95,97,112,113,135# ADH1 (#10# isozyme <202>)
	<156,172,202,215,228,252,282>
SY	#8,101,103,108,138# ADH4 (#108# isozyme <214>) <124,174,177,214,252>
SY	#83# ADH8 <125>
SY	#84# CHY1186 (#84# gene name <226>) <226>
SY	#86# medium chain alcohol dehydrogenase <127>
SY	#9# alcohol dehydrogenase <224>
SY	#9# ADH5 <228>
SY	#9# alcohol dehydrogenase 5 <228>
SY	#92# LSADH <137>

REACTION
RE	a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,40# ordered
	bi-bi mechanism <31,43>; #4,74# rapid equilibrium random mechanism
	<63>; #8# ordered bi bi mechanism with cofactor adding first to form a
	binary enzyme complex <23>; #40# isoenzyme EE and SS: ordered bi bi
	mechanism <35>; #10,32# mechanism is predominantly ordered with
	ethanol, but partially random with butanol <91>; #40# kinetic mechanism
	is random for ethanol oxidation and compulsory ordered for acetaldehyde
	reduction <41>; #37# oxidizes ethanol in an ordered bi-bi mechanism
	with NAD+ as the first substrate fixed <85>; #10# compulsory-order
	mechanism with the rate-limiting step being the dissociation of the
	product enzyme-NAD+ complex <90>; #27,67,77# Theorell-Chance mechanism
	<38,69,74>; #43# sequential reaction mechanism <114>; #86# active site
	structure <127>; #77# catalytic mechanism involves a proton relay
	modulated by the coupled ionization of the active site Lys155/Tyr151
	pair, and a NAD+ ribose 2-OH switch, other active site residues are
	Ser138 and Trp144, ionization properties, substrate binding, overview
	<130>; #8# class IV alcohol dehydrogenase also functions as retinol
	dehydrogenase, reaction and kinetic mechanism: asymmetric rapid
	equilibrium random mechanism with 2 dead-end ternary complexes fro
	retinol oxidation and a rapid equilibrium ordered mechanism with one
	dead-end ternary complex for retinal reduction, a unique mechanistic
	form fro zinc-containing ADH in the medium chain
	dehydrogenase/reductase superfamily of enzymes <124>; #10# detailed
	determination of the reaction and kinetic mechanisms, active site
	structure and determination of amino acid residues involved in
	catalysis, 3 isozymes <120>; #5# ordered bibi mechanism, structural and
	functional implications of amino acid residue 47 <110>; #40# ordered
	sequential bibi reaction mechanism, modeling of oxidation kinetic
	mechanism <117>; #40# reaction mechanism, His51 is involved, but not
	essential, in catalysis facilitating the deprotonation of the hydroxyl
	group of water or alcohol ligated to the catalytic zinc <111>; #8#
	Ser48 is involved in catalysis, isozyme gamma(2)gamma(2) <109>; #26#
	the catalytic triad consists of Cys44, His67, and Cys154, active site
	structure <129>)
RE	a secondary alcohol + NAD+ = a ketone + NADH + H+

REACTION_TYPE
RT	redox reaction
RT	oxidation
RT	reduction

SOURCE_TISSUE
ST	#1,2,5,8,9,12,35,40,42,52,58,68,72,78,79,82,105,129,130# liver (#5#
	isoenzyme A2 and B2 <48>; #35# isoenzyme AA-ADH and BB-ADH most
	abundant in <95>; #8# isozyme ADH1C*2 <116>; #9# females show 70%
	higher hepatic alcohol dehydrogenase activity and display 60% lower
	voluntary ethanol intake than males. Following ethanol administration
	(1 g/kg ip), females generate a transient blood acetaldehyde increase
	with levels that are 2.5fold greater than in males. Castration of males
	leads to an increase alcohol dehydrogenase activity the appearance of
	an acetaldehyde burst a reduction of voluntary ethanol intake
	comparable with that of females <167>; #8# the activities of total
	alcohol dehydrogenase, aldehyde dehydrogenase and class I alcohol
	dehydrogenase isoenzyme between cancer liver tissues and healthy
	hepatocytes might be a factor in ethanol metabolism disorders which can
	intensify carcinogenesis <186>; #105# isozymes ADH1C and ADH3 <214>;
	#8# most abundant in the liver <180>; #8# the total alcohol
	dehydrogenase activity is significantly higher in cancer tissues than
	in healthy liver <194>; #130# class III ADH <227>)
	<1,2,5,10,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31
	32,33,34,35,36,37,39,40,41,42,44,45,46,48,49,51,52,54,55,59,60,86,92,93
	95,98,101,111,116,117,143,167,175,178,180,186,194,198,200,201,204,205
	212,214,224,227,275>
ST	#10,40,70# commercial preparation (#10# lyophilized <122>)
	<117,121,122,148,179,251,261,275,277,278>
ST	#10,93,102,103,157# culture condition:ethanol-grown cell (#93# highest
	ethanol consumption rate in cultures grown on 0.79% w/v ethanol <162>;
	#10# during the biological aging of sherry wines, where Saccharomyces
	bayanus has to grow on ethanol owing to the absence of glucose, this
	isoenzyme plays a prominent role by converting the ethanol into
	acetaldehyde and producing NADH in the process. Overexpression of the
	gene ADH2 (from Saccharomyces cerevisiae) during alcoholic fermentation
	has no effect on the proteomic profile or the net production of some
	metabolites associated with glycolysis and alcoholic fermentation such
	as ethanol, acetaldehyde, and glycerol. However, it affects indirectly
	glucose and ammonium uptakes, cell growth, and intracellular redox
	potential, which lead to an altered metabolome <170>; #102,103#
	significantly expressed in ethanol medium <177>; #157# at pH 6.0 and pH
	3.7 <283>) <162,170,177,283>
ST	#102# culture condition:glycerol-grown cell (#102# strongly expressed
	in glycerol medium <177>) <177>
ST	#105,108# buccal mucosa (#105,108# isozyme ADH4 <214>) <214>
ST	#125# silk gland <231>
ST	#125# ganglion <231>
ST	#125# egg <231>
ST	#125# epidermis <231>
ST	#125# fat body <231>
ST	#125# hemocyte <231>
ST	#125# midgut <231>
ST	#125# malpighian tubule <231>
ST	#125# sperm <231>
ST	#125# hindgut <231>
ST	#16# shoot <79>
ST	#16,124# root (#124# expression of Adh2 in the root apical meristem
	<233>) <79,233>
ST	#16,21,64# leaf (#64# the changes in the carbon metabolism-associated
	proteins reflect altered patterns of carbon flux in response to changes
	in ADH activity in transformed plant leaves <183>) <72,79,183>
ST	#18# scutellum <75>
ST	#18# kernel <97>
ST	#18,124# seedling <76,233>
ST	#19,80# embryo <71,77>
ST	#23# trophozoite <100,123,128>
ST	#3,16,27,31,44,73# seed <4,6,7,73,74,79>
ST	#43# lyophilized cell <232>
ST	#44# coleoptile <80>
ST	#5# blood (#5# ADH3 plays an important role in systemic ethanol
	metabolism at higher levels of blood ethanol through activation by
	cytoplasmic solution hydrophobicity <141>) <141>
ST	#5,8# hepatocyte (#8# the activities of total alcohol dehydrogenase,
	aldehyde dehydrogenase and class I alcohol dehydrogenase isoenzyme
	between cancer liver tissues and healthy hepatocytes might be a factor
	in ethanol metabolism disorders which can intensify carcinogenesis
	<186>) <117,186>
ST	#5,8# retina (#5,8# isozyme ADH4 <119>) <119>
ST	#5,8,9,83# stomach (#5# isoenzyme C2 <48>; #8# stomach mucosa,
	mue-alcohol dehydrogenase <96>; #8# isozymes ADH5 and ADH4, the total
	alcohol dehydrogenase activity is significantly higher in cancer
	tissues than in healthy stomach <194>) <48,49,50,53,96,125,194>
ST	#5,8,9,84,125# more (#5,9# tissue-specific expression patterns of class
	I, III, and IV Adh <142>; #5# ADH3 is expressed ubiquitously and with
	relatively little inter-tissue variation in mammals, in contrast to
	other ADHs <200>; #8# activity of ADH isoenzymes and ALDH in cervical
	carcinoma and healthy tissues., overview <229>; #9# no expression of
	ADH5 in lung, epididymis, uterus, ovary, thymus, adrenal, small
	intestine, heart, eye, muscle, brain, testis, stomach, spleen, and
	liver <228>; #84# optimal growth at 78°C <226>; #125# tissue
	expression profile of fifth instar larvae, overview <231>)
	<142,200,226,228,229,231>
ST	#52# cecum <59>
ST	#53,59# fruit (#59# peel and flesh, alcohol dehydrogenase is
	independent of ethylene modulation <146>; #53# upregulated during
	ripening, the enzyme plays a specific role in the regulation of aroma
	biosynthesis in melon fruit <151>) <146,151>
ST	#8# skin <194>
ST	#8# hepatoma cell <180>
ST	#8# serum <194>
ST	#8# adenocarcinoma cell <229>
ST	#8# aorta (#8# the activity of the class I ADH isoenzyme is
	significantly lower in the wall of aortic aneurysm than in healthy
	aorta <206>) <206>
ST	#8# esophagus (#8# isozyme ADH4, the total alcohol dehydrogenase
	activity is significantly higher in cancer tissues than in healthy
	esophagus <194>) <194>
ST	#8# blood serum (#8# among all tested classes of ADH isoenzymes, only
	class I has higher activity in serum of patients with breast cancer in
	stage IV. The total ADH activity is not significantly higher in
	patients with breast cancer than in healthy controls. The changes in
	activity, especially in class I ADH, appear to be caused by isoenzymes
	being released from the organ damaged by metastatic disease <150>; #8#
	the total ADH activity is significantly higher (44%) among patients
	with cancer than healthy ones. The activity of class I ADH isoenzymes
	is elevated only in the serum of patients with metastatic liver cancer.
	This increase of activity seems to be caused by the enzyme released
	from liver cancer cells and primary tumors originating in other organs
	<186>) <150,186>
ST	#8# colorectum (#8# the total alcohol dehydrogenase activity is
	significantly higher in cancer tissues than in healthy colorectum
	<194>) <194>
ST	#8# cervical cancer cell <229>
ST	#8,9# pancreas (#8# total activity of alcohol dehydrogenase is not
	significantly different in cancer and normal cells. The differences
	between enzymes of drinkers and nondrinkers in both cancer and healthy
	tissue are not significant <191>) <49,191>
ST	#8,9# uterus <49,229>
ST	#8,9# kidney (#8# isozyme ADH1 <194>; #9# high expression level of ADH5
	<228>) <49,194,228>
ST	#8,9# lung (#8# isozyme ADH1 <194>) <49,194>
ST	#8,9# cornea (#8# isozyme ADH4 <194>) <49,194>
ST	#8,9,35# testis (#8# the class III enzyme contributes by far the bulk
	of the total alcohol dehydrogenase activity <11>; #35# isoenzyme TT-ADH
	is only found in testis <95>; #35# activity increases during the
	prepubertal development <47>) <11,47,49,95>
ST	#85# mycelium (#85# aerobically grown <136>) <136>
ST	#89# corm (#89# dormant <105>) <105>
ST	#9# heart <49>
ST	#9# spleen <49>
ST	#9# duodenum (#9# low expression level of ADH5 <228>) <228>
ST	#9# brain <49>
ST	#9# muscle <49>
ST	#9# adrenal gland <49>
ST	#9# colon (#9# low expression level of ADH5 <228>) <228>
ST	#9# thymus <49>
ST	#9# epididymis <49>
ST	#9,125# ovary <49,231>
ST	#9,130# intestine (#130# class III ADH <227>) <49,227>
ST	#90,107# larva <208>
ST	#99# culture condition (#99# adhA transcription is induced by ethanol
	or n-propanol, adhA transcription is subject to glucose catabolite
	repression. Accordingly, both induction of AdhA activity and ethanol
	utilization are detected only after depletion of glucose <171>) <171>

LOCALIZATION
LO	#101# mitochondrial matrix <174>
LO	#23,95# more (#23# detection in the membrane pellet is probably due to
	cosedimentation of the multimeric enzyme during membrane purification
	<128>; #95# no activity can be localized in the periplasm <156>)
	<128,156>
LO	#5# nucleus <200>
LO	#5# extracellular <117>
LO	#5,10,95,112,158# cytoplasm (#95# 68% of total activity measured <156>)
	<156,200,202,209,276,285>
LO	#50,95# membrane (#95# 32% of total activity measured <156>) <156,279>
LO	#7,8,23,26,33,49,60,65,105,108# cytosol (#60# 2 isozymes <113>; #23#
	enzyme polymer forms rod-like helical particles <128>)
	<113,128,135,194,214>
LO	#9# microsome <224>
LO	#9,61,102,103,126,157# mitochondrion (#61# KlDH3 and KlADH4 are genes
	encoding mitochondrial alcohol dehydrogenase activities located within
	the mitochondria. Ethanol induces the transcription of KlADH4 and,
	conversely, represses that of KlADH3 <145>; #102# KmAdh3 possesses an
	amino-terminal extension as a mitochondrial targeting sequence <177>;
	#103# KmAdh4 possesses an amino-terminal extension as a mitochondrial
	targeting sequence <177>; #126# HpADH3 <222>; #157# higher enzyme level
	in mitochondria from cells grown at pH 6.0 than in mitochondria from
	cells grown at pH 3.7 <283>) <145,177,222,224,283>

NATURAL_SUBSTRATE_PRODUCT
NSP	#10,126# acetaldehyde + NADH + H+ = ethanol + NAD+ (#10# cells with an
	extra copy of ADH1 display chronological life-span extension.
	Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an
	extra ADH1 copy show extended replicative life span and increased Sir2p
	activity <190>) {r} <190,222>
NSP	#10,126# acetaldehyde + NADH + H+ = ethanol + NAD+ (#10# cells with an
	extra copy of ADH1 display chronological life-span extension.
	Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an
	extra ADH1 copy show extended replicative life span and increased Sir2p
	activity <190>) {} <190,222>
NSP	#10,126# acetaldehyde + NADH + H+ = ethanol + NAD+ (#10# cells with an
	extra copy of ADH1 display chronological life-span extension.
	Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an
	extra ADH1 copy show extended replicative life span and increased Sir2p
	activity <190>) <190,222>
NSP	#47,124,125,126# ethanol + NAD+ = acetaldehyde + NADH + H+
	<222,223,231,233>
NSP	#47,124,125,126# ethanol + NAD+ = acetaldehyde + NADH + H+ {r}
	<222,223,231,233>
NSP	#47,124,125,126# ethanol + NAD+ = acetaldehyde + NADH + H+ {}
	<222,223,231,233>
NSP	#5# allyl alcohol + NAD+ = acrolein + NADH |#5# product is toxic in
	mouse hepatocytes due to cell protein carbonylation following exposure
	to crotyl alcohol <117>| <117>
NSP	#5# allyl alcohol + NAD+ = acrolein + NADH |#5# product is toxic in
	mouse hepatocytes due to cell protein carbonylation following exposure
	to crotyl alcohol <117>| {r} <117>
NSP	#5# octanol + NAD+ = octanal + NADH <200>
NSP	#5# a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#5# ADH3 is
	involved in multiple cellular pathways, as diverse as formaldehyde
	detoxification, retinoid metabolism and NO homeostasis, ADH3 is
	considered to play only a minor role in hepatic alcohol metabolism
	because ethanol concentrations rarely exceed 50 mM <200>) <200>
NSP	#5,40# crotyl alcohol + NAD+ = crotonaldehyde + NADH (#40# product is
	toxic in mouse hepatocytes due to cell protein carbonylation following
	exposure to crotyl alcohol <117>) |#5# product is toxic in mouse
	hepatocytes due to cell protein carbonylation following exposure to
	crotyl alcohol <117>| <117>
NSP	#5,8# all-trans-retinol + NAD+ = all-trans-retinal + NADH (#8# ADH4
	might be involved in biosynthesis of retinoic acid <124>) <124,200>
NSP	#5,8# all-trans-retinol + NAD+ = all-trans-retinal + NADH (#8# ADH4
	might be involved in biosynthesis of retinoic acid <124>) {r} <124,200>
NSP	#5,8,10,30,40# ethanol + NAD+ = acetaldehyde + NADH (#5# role of the
	major liver isoenzyme A2 in ethanol metabolism <48>; #40# plays an
	important role in the metabolism of ethanol <102>; #8# chi-ADH plays an
	important role in the metabolism of long chain alcohols and aldehydes
	<21>; #8# the anodic enzyme form may contribute significantly to
	alcohol elimination in man, particularly at high concentrations when
	the other enzyme species are saturated <18>; #8# the enzyme plays a
	significant role in first-pass metabolism of ethanol in human <96>; #8#
	enzyme is responsible for the major ethanol oxidation capacity in the
	body. The products acetaldehyde and NADH are responsible for the most
	of the toxic effects and metabolic disturbances produced by ethanol
	ingestion <10>; #10# rate-limiting step of the alcoholic fermentation
	<122>; #5# DH3 plays an important role in systemic ethanol metabolism
	at higher levels of blood ethanol through activation by cytoplasmic
	solution hydrophobicity <141>) {} <10,18,21,48,96,102,116,122,141,181>
NSP	#5,8,10,30,40# ethanol + NAD+ = acetaldehyde + NADH (#5# role of the
	major liver isoenzyme A2 in ethanol metabolism <48>; #40# plays an
	important role in the metabolism of ethanol <102>; #8# chi-ADH plays an
	important role in the metabolism of long chain alcohols and aldehydes
	<21>; #8# the anodic enzyme form may contribute significantly to
	alcohol elimination in man, particularly at high concentrations when
	the other enzyme species are saturated <18>; #8# the enzyme plays a
	significant role in first-pass metabolism of ethanol in human <96>; #8#
	enzyme is responsible for the major ethanol oxidation capacity in the
	body. The products acetaldehyde and NADH are responsible for the most
	of the toxic effects and metabolic disturbances produced by ethanol
	ingestion <10>; #10# rate-limiting step of the alcoholic fermentation
	<122>; #5# DH3 plays an important role in systemic ethanol metabolism
	at higher levels of blood ethanol through activation by cytoplasmic
	solution hydrophobicity <141>) {r} <10,18,21,48,96,102,116,122,141,181>
NSP	#5,8,10,30,40# ethanol + NAD+ = acetaldehyde + NADH (#5# role of the
	major liver isoenzyme A2 in ethanol metabolism <48>; #40# plays an
	important role in the metabolism of ethanol <102>; #8# chi-ADH plays an
	important role in the metabolism of long chain alcohols and aldehydes
	<21>; #8# the anodic enzyme form may contribute significantly to
	alcohol elimination in man, particularly at high concentrations when
	the other enzyme species are saturated <18>; #8# the enzyme plays a
	significant role in first-pass metabolism of ethanol in human <96>; #8#
	enzyme is responsible for the major ethanol oxidation capacity in the
	body. The products acetaldehyde and NADH are responsible for the most
	of the toxic effects and metabolic disturbances produced by ethanol
	ingestion <10>; #10# rate-limiting step of the alcoholic fermentation
	<122>; #5# DH3 plays an important role in systemic ethanol metabolism
	at higher levels of blood ethanol through activation by cytoplasmic
	solution hydrophobicity <141>) <10,18,21,48,96,102,116,122,141,181>
NSP	#8# isobutyramide + NAD+ = ? {r} <124>
NSP	#8# 1-butanol + NAD+ = butanal + NADH + H+ <229>
NSP	#8# 1-butanol + NAD+ = butanal + NADH + H+ {r} <229>
NSP	#8,10,35,40,41,51,52,59,77,111,122# more = ? (#10# constitutive enzyme
	<94>; #41# key enzyme in ethanol production <68>; #51# one constitutive
	enzyme, ADH-MI and one inducible enzyme, ADH-MII <82>; #52# enzyme may
	be involved in the metabolism of dietary wax esters in salmonid fish
	<59>; #77# the enzyme oxidizes alcohols to aldehydes or ketones both
	for detoxification and metabolic purposes <38>; #35# involvement in the
	development of male hamster reproductive system <47>; #59# alcohol
	dehydrogenase activity may not limit alcohol supply for ester
	production during ripening <146>; #40# activity is severely reduced
	towards aliphatic alcohols of more than 8 carbon atoms for the free
	enzyme, but not so with immobilized HLAD, exhibiting an activity
	towards C22 and C24 aliphatic alcohols higher than 50% of the highest
	value, obtained with C8 <204>; #8# differences in the activities of
	total ADH and class I ADH isoenzyme between cancer liver tissues and
	healthy hepatocytes may be a factor in ethanol metabolism disorders,
	which can intensify carcinogenesis <180>; #111# TADH is a
	NAD(H)-dependent enzyme and shows a very broad substrate spectrum
	producing exclusively the (S)-enantiomer in high enantiomeric excess
	(more than 99%) during asymmetric reduction of ketones <197>; #122# the
	physiological direction of the catalytic reaction is reduction rather
	than oxidation <219>) {} <38,47,59,68,82,94,146,180,197,204,219>
NSP	#8,10,35,40,41,51,52,59,77,111,122# more = ? (#10# constitutive enzyme
	<94>; #41# key enzyme in ethanol production <68>; #51# one constitutive
	enzyme, ADH-MI and one inducible enzyme, ADH-MII <82>; #52# enzyme may
	be involved in the metabolism of dietary wax esters in salmonid fish
	<59>; #77# the enzyme oxidizes alcohols to aldehydes or ketones both
	for detoxification and metabolic purposes <38>; #35# involvement in the
	development of male hamster reproductive system <47>; #59# alcohol
	dehydrogenase activity may not limit alcohol supply for ester
	production during ripening <146>; #40# activity is severely reduced
	towards aliphatic alcohols of more than 8 carbon atoms for the free
	enzyme, but not so with immobilized HLAD, exhibiting an activity
	towards C22 and C24 aliphatic alcohols higher than 50% of the highest
	value, obtained with C8 <204>; #8# differences in the activities of
	total ADH and class I ADH isoenzyme between cancer liver tissues and
	healthy hepatocytes may be a factor in ethanol metabolism disorders,
	which can intensify carcinogenesis <180>; #111# TADH is a
	NAD(H)-dependent enzyme and shows a very broad substrate spectrum
	producing exclusively the (S)-enantiomer in high enantiomeric excess
	(more than 99%) during asymmetric reduction of ketones <197>; #122# the
	physiological direction of the catalytic reaction is reduction rather
	than oxidation <219>) {} <38,47,59,68,82,94,146,180,197,204,219>

SUBSTRATE_PRODUCT
SP	#10# n-propanol + NAD+ = n-propanal + NADH {r} <120>
SP	#10# 2-propanol + NAD+ = acetone + NADH <122>
SP	#10# n-hexanol + NAD+ = n-hexanal + NADH {r} <120>
SP	#10# (S)-2-butanol + NAD+ = 2-butanone + NADH {r} <120>
SP	#10# ethylenglycol + NAD+ = ? + NADH {r} <120>
SP	#10# n-butanol + NAD+ = butyraldehyde + NADH <122>
SP	#10# n-decanol + NAD+ = n-decanal + NADH {r} <120>
SP	#10# Tris + NAD+ = ? + NADH {r} <120>
SP	#10# isopropanol + NAD+ = acetone + NADH + H+ <139,211>
SP	#10# 5-hydroxymethylfurfural + NADH + H+ = (furan-2,5-diyl)dimethanol +
	NAD+ (#10# mutant enzyme S109P/L116S/Y294C <193>; #10# no substrate for
	wild-type, reaction is catalyzed by mutants Y295C and S110P/Y295C
	<282>) <193,282>
SP	#10# ethanol + beta-NAD+ = acetaldehyde + NADH + H+ <192>
SP	#10# furfural + NADH + H+ = furfuryl alcohol + NADH (#10# mutant enzyme
	S109P/L116S/Y294C <193>) <193,282,285>
SP	#10# phenylglyoxylic acid + NADH + H+ = hydroxy(phenyl)acetic acid +
	NAD+ (#10# enzyme covalently immobilized to magnetic Fe3O4
	nanoparticles via glutaraldehyde retains 48.77% activity of its
	original activity <182>) <182>
SP	#10# ethyl 3-oxobutyrate + NADH + H+ = ethyl (S)-3-hydroxybutyrate +
	NAD+ {} <196>
SP	#10# butanal + NADH = n-butanol + NAD+ <285>
SP	#10# glycolaldehyde + NADH + H+ = glycol + NAD+ <285>
SP	#10# propanal + NADH + H+ = propanol + NAD+ <285>
SP	#10,104# isobutyraldehyde + NADH + H+ = isobutanol + NAD+ <207,285>
SP	#10,104# isobutyraldehyde + NADH + H+ = isobutanol + NAD+ {r} <207,285>
SP	#10,112# (R,S)-2-methylbutan-1-ol + NAD+ = (R,S)-2-methyl-butan-1-one +
	NADH + H+ <202>
SP	#10,112# 2-methylpropan-1-ol + NAD+ = 2-methyl-propan-1-one + NADH + H+
	<202>
SP	#10,112# 3-methylbutan-1-ol + NAD+ = 3-methyl-butan-1-one + NADH + H+
	<202>
SP	#10,112# p-methoxybenzyl alcohol + NAD+ = p-methoxybenzaldehyde + NADH
	+ H+ {r} <202>
SP	#10,112# pentanol + NAD+ = pentanal + NADH + H+ <202>
SP	#10,25,92,104,112# (R)-2-butanol + NAD+ = 2-butanone + NADH + H+ (#92#
	50% of the activity with 2-propanol <137>; #25# 55% of activity with
	N-benzyl-3-pyrrolidinol <188>) <137,188,202,207>
SP	#10,25,92,104,112# (R)-2-butanol + NAD+ = 2-butanone + NADH + H+ (#92#
	50% of the activity with 2-propanol <137>; #25# 55% of activity with
	N-benzyl-3-pyrrolidinol <188>) {r} <137,188,202,207>
SP	#10,25,92,104,112# (R)-2-butanol + NAD+ = 2-butanone + NADH + H+ (#92#
	50% of the activity with 2-propanol <137>; #25# 55% of activity with
	N-benzyl-3-pyrrolidinol <188>) {ir} <137,188,202,207>
SP	#10,40# n-propanol + NAD+ = propanal + NADH <111,122>
SP	#10,40,111,112,129# octanol + NAD+ = octanal + NADH + H+ (#40#
	immobilized and free HLAD show 100% reaction rate with octanol compared
	to ethanol at pH 8.8 and 30°C <204>) |#111# 178% activity compared to
	cyclohexanone <197>| <197,202,204,227>
SP	#10,40,111,112,129# octanol + NAD+ = octanal + NADH + H+ (#40#
	immobilized and free HLAD show 100% reaction rate with octanol compared
	to ethanol at pH 8.8 and 30°C <204>) |#111# 178% activity compared to
	cyclohexanone <197>| {r} <197,202,204,227>
SP	#10,70# 2-propanol + NAD(P)+ = acetone + NAD(P)H <121>
SP	#10,77,112# (S)-2-methylbutan-1-ol + NAD+ = (S)-2-methyl-butanal + NADH
	+ H+ <61,202>
SP	#10,77,112# (S)-2-methylbutan-1-ol + NAD+ = (S)-2-methyl-butanal + NADH
	+ H+ {} <61,202>
SP	#10,92,104,112# (S)-2-butanol + NAD+ = 2-butanone + NADH + H+ (#92#
	275% of the activity with 2-propanol <137>) <137,202,207>
SP	#10,92,104,112# (S)-2-butanol + NAD+ = 2-butanone + NADH + H+ (#92#
	275% of the activity with 2-propanol <137>) {r} <137,202,207>
SP	#10,92,104,112# (S)-2-butanol + NAD+ = 2-butanone + NADH + H+ (#92#
	275% of the activity with 2-propanol <137>) {ir} <137,202,207>
SP	#100# 1,3-butanediol + NAD+ = ? (#100# 39% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 1,2-hexanediol + NAD+ = ? (#100# 20% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 1,2-pentanediol + NAD+ = ? (#100# 12% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 1-hexanol + NAD+ = ? (#100# 15% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 1-hydroxy-2-butanone + NADH + H+ = butane-1,2-diol + NAD+ (#100#
	59% of the activity with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# 1-pentanol + NAD+ = pentanal + NADH + H* (#100# 8% of the
	activity with (S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 1-phenyl-1-propanol + NAD+ = ? (#100# 31% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 2,3-butanediol + NAD+ = ? (#100# 83% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>) <185>
SP	#100# 2,3-butanedione + NADH + H+ = ? (#100# activity is 1.6fold higher
	than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# 2-hexanone + NADH + H+ = ? (#100# activity is 1.6fold higher than
	with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# 3,4-hexanedione + NADH + H+ = ? (#100# 77% of the activity with
	N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# acetylacetone + NADH + H+ = ? (#100# 63% of the activity with
	N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# cyclohexanone + NADH + H+ = ? (#100# activity is 2.1fold higher
	than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# hydroxyacetone + NADH + H+ = propane-1,2-diol + NAD+ (#100# 27%
	of the activity with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# N-benzyl-3-pyrrolidinol + NAD+ = 1-benzylpyrrolidin-3-one + NADH
	+ H+ (#100# 33% of the activity with (S)-N-benzyl-3-pyrrolidinol <185>)
	<185>
SP	#100# n-butylaldehyde + NADH + H+ = butanal + NAD+ (#100# activity is
	1.8fold higher than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# n-hexylaldehyde + NADH + H+ = hexanal + NAD+ (#100# activity is
	1.6fold higher than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# n-octylaldehyde + NADH + H+ = n-octanol + NAD+ (#100# activity is
	1.7fold higher than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# n-valeraldehyde + NADH + H+ = n-pentanol + NAD+ (#100# activity
	is 2.8fold higher than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100# propionaldehyde + NADH + H+ = ? (#100# activity is 1.1fold higher
	than with N-benzyl-3-pyrrolidinone <185>) <185>
SP	#100,111# 2,4-pentanediol + NAD+ = ? (#100# 21% of the activity with
	(S)-N-benzyl-3-pyrrolidinol <185>; #111# 4% activity compared to
	cyclohexanol <197>) <185,197>
SP	#100,126# 1,2-butanediol + NAD+ = ? (#126# low activity <222>; #100#
	35% of the activity with (S)-N-benzyl-3-pyrrolidinol <185>) <185,222>
SP	#100,127# 2-butanone + NADH + H+ = 2-butanol + NAD+ (#100# 40% of the
	activity with N-benzyl-3-pyrrolidinone <185>) {r} <185,225>
SP	#100,127# benzylacetone + NADH + H+ = 4-phenylbutan-2-ol + NAD+ (#100#
	activity is 1.3fold higher than with N-benzyl-3-pyrrolidinone <185>)
	{r} <185,225>
SP	#100,127# benzylacetone + NADH + H+ = 4-phenylbutan-2-ol + NAD+ (#100#
	activity is 1.3fold higher than with N-benzyl-3-pyrrolidinone <185>)
	<185,225>
SP	#104# 1-heptanol + NAD+ = 1-heptanal + NADH + H+ {r} <207>
SP	#104# 2-ethoxyethanol + NAD+ = 2-ethoxyacetaldehyde + NADH + H+ {r}
	<207>
SP	#104# n-butanol + NAD+ = butyraldehyde + NADH + H+ {r} <207>
SP	#104# pentan-3-ol + NAD+ = 3-pentanone + NADH + H+ {r} <207>
SP	#104# 2-(3,5-dimethylphenyl)propanal + NADH + H+ =
	(S)-2-(3,5-dimethylphenyl)propanol + NAD+ (#104# 18 h, 99% yield, 90%
	enantiomeric excess <235>) <235>
SP	#104# 2-(3-benzoylphenyl)propanal + NADH + H+ =
	(S)-2-(3-benzoylphenyl)propanol + NAD+ (#104# 18 h, 85% yield, 95%
	enantiomeric excess <235>) <235>
SP	#104# 2-(3-fluorobiphenyl-4-yl)propanal + NADH + H+ =
	(S)-2-(3-(fluoro)biphenyl-4-yl)propanol + NAD+ (#104# 18 h, 77% yield,
	97% enantiomeric excess <235>) <235>
SP	#104# 2-(3-phenoxyphenyl)propanal + NADH + H+ =
	(S)-2-((3-phenoxy)phenyl)propanol + NAD+ (#104# 18 h, 85% yield, 95%
	enantiomeric excess <235>) <235>
SP	#104# 2-(4-isobutylphenyl)propanal + NADH + H+ =
	(S)-2-(4-isobutylphenyl)propanol + NAD+ (#104# 18 h, 92% yield, 99%
	enantiomeric excess <235>) <235>
SP	#104# 2-(4-trifluoromethylphenyl)propanal + NADH + H+ =
	(S)-2-(4-trifluoromethyl)phenylpropanol + NAD+ (#104# 18 h, 55% yield,
	98% enantiomeric excess <235>) <235>
SP	#104# 2-(6-methoxynaphthalen-2-yl)propanal + NADH + H+ =
	(S)-2-(6-methoxynaphthalen-2-yl)propan-1-ol + NAD+ (#104# 18 h, 96%
	yield, 98% enantiomeric excess <235>) <235>
SP	#104# 2-(naphthalen-1-yl)propanal + NADH + H+ =
	(S)-2-(naphthalen-1-yl)propanol + NAD+ (#104# 18 h, 90% yield, 80%
	enantiomeric excess <235>) <235>
SP	#104# 2-(naphthalen-2-yl)propanal + NADH + H+ =
	(S)-2-(naphthalen-2-yl)propanol + NAD+ (#104# 18 h, 57% yield, 94%
	enantiomeric excess <235>) <235>
SP	#104# 2-phenylpropanal + NADH + H+ = (S)-2-phenylpropanol + NAD+ (#104#
	18 h, 74% yield, 98% enantiomeric excess <235>) <235>
SP	#104# 2-[3-(2-phenyl-1,3-dioxolan-2-yl)phenyl]propanal + NADH + H+ =
	(S)-2-(3-(2-phenyl-1,3-dioxolan-2-yl)phenyl)propanol + NAD+ (#104# 18
	h, 95% yield, 61% enantiomeric excess <235>) <235>
SP	#104,111# 3-pentanol + NAD+ = 3-pentanone + NADH + H+ (#111# 2%
	activity compared to cyclohexanol <197>) |#111# 2% activity compared to
	cyclohexanone <197>| {r} <197,207>
SP	#104,131# 1-hexanol + NAD+ = 1-hexanal + NADH + H+ {r} <207,239>
SP	#104,131# 1-hexanol + NAD+ = 1-hexanal + NADH + H+ <207,239>
SP	#104,131# 1-pentanol + NAD+ = 1-pentanal + NADH + H+ {r} <207,239>
SP	#104,131# 1-pentanol + NAD+ = 1-pentanal + NADH + H+ <207,239>
SP	#105,108# 1-hydroxymethyl-6-methylpyrene + NAD+ =
	1-formyl-6-methylpyrene + NADH + H+ {r} <214>
SP	#105,108# 1-hydroxymethyl-8-methylpyrene + NAD+ =
	1-formyl-8-methylpyrene + NADH + H+ {r} <214>
SP	#105,108# 1-hydroxymethylpyrene + NAD+ = 1-formylpyrene + NADH + H+ {r}
	<214>
SP	#105,108# 2-hydroxymethylpyrene + NAD+ = 2-formylpyrene + NADH + H+ {r}
	<214>
SP	#105,108# 4-hydroxymethylpyrene + NAD+ = 4-formylpyrene + NADH + H+ {r}
	<214>
SP	#111# (-)-carvone + NADH + H+ = ? + NAD+ (#111# 1% activity compared to
	cyclohexanone <197>) <197>
SP	#111# (1S,3S)-3-methylcyclohexanol + NAD+ = (rac)-3-methylcyclohexanone
	+ NADH + H+ (#111# 125% activity compared to cyclohexanol <197>) |#111#
	163% activity compared to cyclohexanone <197>| {r} <197>
SP	#111# (R)-3-methylcyclohexanone + NADH + H+ = ? + NAD+ (#111# 2%
	activity compared to cyclohexanone <197>) <197>
SP	#111# (S)-1-phenyl-2-propanol + NAD+ = phenylacetone + NADH + H+ |#111#
	9% activity compared to cyclohexanone <197>| {r} <197>
SP	#111# (S)-4-phenylbutan-2-ol + NAD+ = benzylacetone + NADH + H+ |#111#
	3% activity compared to cyclohexanone <197>| {r} <197>
SP	#111# (S)-heptan-2-ol + NAD+ = 2-heptanone + NADH + H+ {r} <197>
SP	#111# (S)-pentan-2-ol + NAD+ = 2-pentanone + NADH + H+ {r} <197>
SP	#111# (S)-perillylalcohol + NAD+ = (S)-perillaldehyde + NADH + H+
	(#111# 52% activity compared to cyclohexanol <197>) <197>
SP	#111# 1-(p-tolyl)-ethanol + NAD+ = 1-(4-methylphenyl)ethanone + NADH +
	H+ (#111# 19% activity compared to cyclohexanol <197>) |#111# 26%
	activity compared to cyclohexanone <197>| <197>
SP	#111# 1-phenyl-1,2-ethanediol + NAD+ = 1-phenyl-2-propanone + NADH + H+
	(#111# 1% activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 1-phenylethanol + NAD+ = acetophenone + NADH + H+ |#111# 1%
	activity compared to cyclohexanone <197>| <197>
SP	#111# 2-chlorocyclohexanone + NADH + H+ = ? + NAD+ (#111# 3% activity
	compared to cyclohexanone <197>) <197>
SP	#111# 2-decalone + NADH + H+ = ? + NAD+ (#111# 28% activity compared to
	cyclohexanone <197>) <197>
SP	#111# 2-methyl-2,4-pentanediol + NAD+ = ? (#111# 1% activity compared
	to cyclohexanol <197>) <197>
SP	#111# 2-methylcyclohexanone + NADH + H+ = ? + NAD+ (#111# 46% activity
	compared to cyclohexanone <197>) <197>
SP	#111# 2-phenylcyclohexanone + NADH + H+ = ? + NAD+ (#111# 2% activity
	compared to cyclohexanone <197>) <197>
SP	#111# 2-phenylethanol + NAD+ = 2-phenylethanone + NADH + H+ (#111# 57%
	activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 3,3,5-trimethylcyclohexanone + NADH + H+ = ? + NAD+ (#111# 2%
	activity compared to cyclohexanone <197>) <197>
SP	#111# 3,4-dimethylbenzyl alcohol + NAD+ = 3,4-dimethylbenzaldehyde +
	NADH + H+ (#111# 45% activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 3,5-dimethylcyclohexanol + NAD+ = 3,5-dimethylcyclohexanone +
	NADH + H+ (#111# 1% activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 3-aminobenzyl alcohol + NAD+ = 3-aminobenzaldehyde + NADH + H+
	(#111# 8% activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 3-methyl-2-cyclohexenone + NADH + H+ = ? + NAD+ (#111# 1%
	activity compared to cyclohexanone <197>) <197>
SP	#111# 3-methylbutanol + NAD+ = 3-methylbutanone + NADH + H+ (#111# 133%
	activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 3-methylphenylethyl alcohol + NAD+ = ? (#111# 64% activity
	compared to cyclohexanol <197>) <197>
SP	#111# 3-penten-2-one + NADH + H+ = ? + NAD+ (#111# 2% activity compared
	to cyclohexanone <197>) <197>
SP	#111# 4-ethylcyclohexanol + NAD+ = 4-ethylcyclohexanone + NADH + H+
	(#111# 60% activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 4-ethylcyclohexanone + NADH + H+ = ? + NAD+ (#111# 22% activity
	compared to cyclohexanone <197>) <197>
SP	#111# 4-methylcyclohexanol + NAD+ = 4-methylcyclohexanone + NADH + H+
	(#111# 56% activity compared to cyclohexanol <197>) {r} <197>
SP	#111# 4-methylcyclohexanone + NADH + H+ = ? + NAD+ (#111# 25% activity
	compared to cyclohexanone <197>) <197>
SP	#111# acetylacetone + NADH + H+ = acetophenone + NADH + H+ (#111# 1%
	activity compared to cyclohexanone <197>) |#111# 1% activity compared
	to cyclohexanone <197>| {r} <197>
SP	#111# cyclopentanone + NADH + H+ = ? + NAD+ (#111# 1% activity compared
	to cyclohexanone <197>) <197>
SP	#111# decahydro-2-naphthol + NAD+ = ? (#111# 37% activity compared to
	cyclohexanol <197>) <197>
SP	#111# isopropanol + NAD+ = 2-propanone + NADH + H+ {r} <197>
SP	#111# pentanol + NAD+ = valeraldehyde + NADH + H+ |#111# 240% activity
	compared to cyclohexanone <197>| {r} <197>
SP	#111# tetrahydro-4H-pyran-4-one + NADH + H+ = ? + NAD+ (#111# 10%
	activity compared to cyclohexanone <197>) <197>
SP	#111,127# 2-pentanone + NADH + H+ = 2-pentanol + NAD+ (#111# 6%
	activity compared to cyclohexanol <197>) {r} <197,225>
SP	#111,149# 1-phenylethanol + NAD+ = 1-phenylethanone + NADH + H+ (#111#
	3% activity compared to cyclohexanol <197>) <197,243>
SP	#111,149# 1-phenylethanol + NAD+ = 1-phenylethanone + NADH + H+ (#111#
	3% activity compared to cyclohexanol <197>) {r} <197,243>
SP	#113# ethanol + 2 NADP+ + H2O = acetic acid + 2 NADPH + 2 H+ {r} <215>
SP	#113# glycerol + 2 NAD+ + H2O = ? + 2 NADH + 2 H+ (#113# about 45% of
	the activity with ethanol <215>) {r} <215>
SP	#113,114# 1,3-propanediol + 2 NAD+ + H2O = ? + 2 NADH + 2 H+ (#113#
	about 45% of the activity with ethanol <215>; #114# about 5% of the
	activity with 1-octanol <215>) {r} <215>
SP	#113,114# 1-butanol + 2 NAD+ + H2O = butanoic acid + 2 NADH + 2 H+
	(#113# about 45% of the activity with ethanol <215>; #114# about 50% of
	the activity with 1-octanol <215>) {r} <215>
SP	#113,114# 1-hexanol + 2 NAD+ + H2O = hexanoic acid + 2 NADH + 2 H+
	(#114# about 55% of the activity with 1-octanol <215>; #113# about 70%
	of the activity with ethanol <215>) {r} <215>
SP	#113,114# 1-octanol + 2 NAD+ + H2O = octanoic acid + 2 NADH + 2 H+
	(#114# best substrate <215>; #113# about 30% of the activity with
	ethanol <215>) {r} <215>
SP	#113,114# ethanol + 2 NAD+ + H2O = acetic acid + 2 NADH + 2 H+ (#113#
	best substrate <215>; #114# about 45% of the activity with 1-octanol
	<215>) {r} <215>
SP	#114# octanal + NAD+ + H2O = octanoic acid + NADH + H+ (#114# about 25%
	of the activity with 1-octanol <215>) {r} <215>
SP	#114# 1-octanol + 2 NADP+ + H2O = octanoic acid + 2 NADPH + 2 H+ {r}
	<215>
SP	#114# acetone + NAD+ + H2O = ? + NADH + H+ (#114# about 5% of the
	activity with 1-octanol <215>) {r} <215>
SP	#114# isoamylalcohol + 2 NAD+ + H2O = ? + 2 NADH + 2 H+ (#114# about 5%
	of the activity with 1-octanol <215>) {r} <215>
SP	#114# isopropanol + 2 NAD+ + H2O = ? + 2 NADH + 2 H+ (#114# about 10%
	of the activity with 1-octanol <215>; #114# about 15% of the activity
	with 1-octanol <215>) {r} <215>
SP	#114# methanol + 2 NAD+ + H2o = formic acid + 2 NADH + 2 H+ (#114#
	about 25% of the activity with 1-octanol <215>) {r} <215>
SP	#114# octanoic acid + 2 NADH + 2 H+ = 1-octanol + 2 NAD+ + H2o {r} <215>
SP	#114,148# acetaldehyde + NADH + H+ = ethanol + NAD+ + H+ {r} <215,241>
SP	#114,148# acetaldehyde + NADH + H+ = ethanol + NAD+ + H+ <215,241>
SP	#118# 12-hydroxylauric acid methyl ester + NAD+ = 12-oxo lauricacid
	methyl ester + NADH + H+ |#118# product is a key intermediate for
	biobased polyamide 12 production <246>| <246>
SP	#118# 12-oxolauric acid methyl ester + NADH + H+ = 12-hydroxylauric
	acid methyl ester + NAD+ <246>
SP	#118# 4-methoxybenzaldehyde + NADH + H+ = 4-methoxybenzyl alcohol +
	NAD+ |#118# 51% of the activity with butan-2-ol <256>| <256>
SP	#118# butan-2-ol + NAD+ = butanone + NADH + H+ |#118# 83% of the
	activity with butan-2-ol <256>| <256>
SP	#118# butyraldehyde + NAD+ = n-butanol + NADH + H+ {r} <246>
SP	#118# n-butanol + NADH + H+ = butyraldehyde + NAD+ {r} <246>
SP	#118# prop-2-en-1-ol + NAD+ = prop-2-enal + NADH + H+ |#118# 85% of the
	activity with butan-2-ol <256>| <256>
SP	#118# propan-2-ol+ NAD+ = acetone + NADH + H+ |#118# 79% of the
	activity with butan-2-ol <256>| <256>
SP	#118# propanal + NADH + H+ = propan-1-ol + NAD+ |#118# 38% of the
	activity with butan-2-ol <256>| {r} <256>
SP	#118,123# cyclopentanol + NAD+ = cyclopentanone + NADH + H+ (#123# 55%
	of the activity compared to isoborneol <218>) |#118# 92% of the
	activity with butan-2-ol <256>| <218,256>
SP	#118,142# pentan-2-ol + NAD+ = pentan-2-one + NADH + H+ |#142# 9% of
	the activity with 2,3-butanediol <138>; #118# 93% of the activity with
	butan-2-ol <256>| <138,256>
SP	#122# ethyl pyruvate + NADH = ? (#122# about 15% of the activity
	compared to isatin <219>) <219>
SP	#122# methyl benzoylformate + NADH = ? (#122# about 35% of the activity
	compared to isatin <219>) <219>
SP	#122# isatin + NADH = ? <219>
SP	#122# (R)-1-indanol + NAD+ = ? (#122# 62% of activity compared to
	(S)-1-indanol <219>) <219>
SP	#122# (R)-alpha-tetralol + NAD+ = ? (#122# 58% of activity compared to
	(S)-1-indanol <219>) <219>
SP	#122# (S)-1-indanol + NAD+ = ? <219>
SP	#122# (S)-2-pentanol + NAD+ = ? (#122# 11% of activity compared to
	(S)-1-indanol <219>) <219>
SP	#122# (S)-alpha-tetralol + NAD+ = ? (#122# 12% of activity compared to
	(S)-1-indanol <219>) <219>
SP	#122# 1-phenyl-1,2-propanedione + NADH = ? (#122# about 25% of the
	activity compared to isatin <219>) <219>
SP	#122# 2,2,2-trifluoroacetophenone + NADH =
	2,2,2-trifluoro-1-phenylethanol + NAD+ (#122# about 35% of the activity
	compared to isatin <219>) <219>
SP	#122# 3-methylcyclohexanol + NAD+ = 3-methylcyclohexanone + NADH + H+
	(#122# 14% of activity compared to (S)-1-indanol <219>) <219>
SP	#122# cis-decahydro-1-naphthol + NAD+ = ? (#122# 11% of activity
	compared to (S)-1-indanol <219>) <219>
SP	#122# ethyl benzoylformate + NADH = ? (#122# about 30% of the activity
	compared to isatin <219>) <219>
SP	#122# methyl o-chlorobenzoylformate + NADH = ? (#122# about 55% of the
	activity compared to isatin <219>) <219>
SP	#122,123# cycloheptanol + NAD+ = cycloheptanone + NADH + H+ (#122# 37%
	of activity compared to (S)-1-indanol <219>) <218,219>
SP	#122,123# cycloheptanol + NAD+ = cycloheptanone + NADH + H+ (#122# 37%
	of activity compared to (S)-1-indanol <219>) {r} <218,219>
SP	#123# 1-indanone + NADH + H+ = (S)-1-indanol + NAD+ |#123# 6 h, 50°C,
	6% conversion, 25% enantiomeric excess <219>| {r} <219>
SP	#123# ethyl benzoylformate + NADH + H+ = ethyl (R)-mandelate + NAD+
	|#123# 50% enantiomeric excess <219>| {r} <219>
SP	#123# isatin + NADH + H+ = ? + NAD+ {r} <219>
SP	#123# 1-decalone + NADH + H+ = decahydronaphthalen-1-ol + NAD+ (#123#
	85% of the activity compared to 1-phenyl-1,2-propanedione <218>) <218>
SP	#123# 2',3',4',5',6'-pentafluoroacetophenone + NADH + H+ =
	1-(2,3,4,5,6-pentafluorophenyl)ethanol + NAD+ (#123# 45% of the
	activity compared to 1-phenyl-1,2-propanedione <218>) <218>
SP	#123# 2,2'-dichlorobenzil + NADH + H+ =
	1,2-bis(2-chlorophenyl)-2-hydroxyethanone + NAD+ <218>
SP	#123# 2-methylcyclohexanone + NADH + H+ = 2-methylcyclohexanol + NAD+
	(#123# 13% of the activity compared to 1-phenyl-1,2-propanedione <218>)
	<218>
SP	#123# 3-methylcyclohexanol + NAD+ = ? (#123# 10% of the activity
	compared to isoborneol <218>) <218>
SP	#123# 3-methylcyclohexanone + NADH + H+ = 3-methylcyclohexanol + NAD+
	(#123# 33% of the activity compared to 1-phenyl-1,2-propanedione <218>)
	<218>
SP	#123# 4-methylcyclohexanone + NADH + H+ = 4-methylcyclohexanol + NAD+
	(#123# 60% of the activity compared to 1-phenyl-1,2-propanedione <218>)
	<218>
SP	#123# tetralin-1-ol + NAD+ = 3,4-dihydronaphthalen-1(2H)-one + NADH +
	H+ (#123# 51% of the activity compared to isoborneol <218>) <218>
SP	#123# benzil + NADH + H+ = (R)-benzoin + NAD+ (#123# 62% of the
	activity compared to 1-phenyl-1,2-propanedione. The enzyme catalyses
	the asymmetric reduction of benzil to (R)-benzoin with both excellent
	conversion (98%) and optical purity (98%) by way of an efficient in
	situ NADH-recycling system involving a second thermophilic ADH <218>)
	<218>
SP	#123# ethyl 3-methyl-2-oxobutyrate + NADH + H+ = ? (#123#
	1-phenyl-1,2-propanedione and ethyl 3-methyl-2-oxobutyrate are the best
	substrate in the reduction reaction <218>) <218>
SP	#123# ethyl benzoylformate + NADH + H+ = ? (#123# 23% of the activity
	compared to 1-phenyl-1,2-propanedione <218>) <218>
SP	#123# ethyl pyruvate + NADH + H+ = ethyl 2-hydroxypropionate + NAD+
	(#123# 16% of the activity compared to 1-phenyl-1,2-propanedione <218>)
	<218>
SP	#123# isoborneol + NAD+ = ? (#123# isoborneol is the best substrate in
	the oxidation reaction <218>) <218>
SP	#123# (R)-1-indanol + NAD+ = 1-indanone + NADH + H+ {r} <219>
SP	#123# (R)-alpha-tetralol + NAD+ = alpha-tetralone + NADH + H+ {r} <219>
SP	#123# methyl benzoylformate + NADH + H+ = methyl (S)-mandelate + NAD+
	|#123# 6 h, 100% conversion, 17% enantiomeric excess <219>| {r} <219>
SP	#123# methyl o-chlorobenzoylformate + NADH + H+ = methyl
	(R)-o-chloromandelate + NAD+ |#123# 6 h, 99% conversion, 72%
	enantiomeric excess <219>| {r} <219>
SP	#126# 2-methoxyethanol + NAD+ = 2-methoxyacetaldehyde + NADH + H+ {r}
	<222>
SP	#127# 1-butanal + NADH + H+ = 1-butanol + NAD+ {r} <225>
SP	#127# 1-chloro-5-acetylfuro[2,3-c]pyridine + NADH + H+ =
	1-chloro-5-(1-hydroxyethyl)furo[2,3-c]pyridine + NAD+ {r} <225>
SP	#127# 1-hexanal + NADH + H+ = 1-hexanol + NAD+ {r} <225>
SP	#127# 2,3'-dichloroacetophenone + NADH + H+ =
	2-chloro-1-(3-chlorophenyl)ethanol + NAD+ {r} <225>
SP	#127# 2-acetylcyclohexanone + NADH + H+ = 2-acetylcyclohexanol + NAD+
	{r} <225>
SP	#127# 2-acetylcyclopentanone + NADH + H+ = 2-acetylcyclopentanol + NAD+
	{r} <225>
SP	#127# 2-acetylfuran + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# 2-acetylpyridine + NADH + H+ = (R)-1-(2-pyridyl)ethanol + NAD+
	{r} <225>
SP	#127# 2-acetylpyrrole + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# 2-acetylthiazole + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# 2-acetylthiophene + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# 2-chloroacetophenone + NADH + H+ = 1-(2-chlorophenyl)ethanol +
	NAD+ (#127# low activity <225>) {r} <225>
SP	#127# 2-hexanone + NADH + H+ = 2-hexanol + NAD+ {r} <225>
SP	#127# 2-nitrobenzaldehyde + NADH + H+ = 2-nitrobenzyl alcohol + NAD+
	(#127# low activity <225>) {r} <225>
SP	#127# 2-octanone + NADH + H+ = 2-octanol + NAD+ {r} <225>
SP	#127# 2-oxopentanoate + NADH + H+ = 2-hydroxypentanoate + NAD+ (#127#
	low activity <225>) {r} <225>
SP	#127# 3-acetylpyridine + NADH + H+ = (R)-1-(3-pyridyl)ethanol + NAD+
	{r} <225>
SP	#127# 3-chlorobenzaldehyde + NADH + H+ = 3-chlorobenzyl alcohol + NAD+
	{r} <225>
SP	#127# 3-methylbutan-2-one + NADH + H+ = 3-methyl-2-butanol + NAD+ {r}
	<225>
SP	#127# 3-nitroacetophenone + NADH + H+ = 1-(3-nitrophenyl)ethanol + NAD+
	{r} <225>
SP	#127# 4-acetylpyridine + NADH + H+ = (R)-1-(4-pyridyl)ethanol + NAD+
	{r} <225>
SP	#127# 4-chloroacetophenone + NADH + H+ = 1-(4-chlorophenyl)ethanol +
	NAD+ {r} <225>
SP	#127# 4-chlorobenzaldehyde + NADH + H+ = 4-chlorobenzyl alcohol + NAD+
	{r} <225>
SP	#127# 4-fluoroacetophenone + NADH + H+ = 1-(4-fluorophenyl)ethanol +
	NAD+ {r} <225>
SP	#127# 4-methylpentan-2-one + NADH + H+ = 4-methyl-2-pentanol + NAD+ {r}
	<225>
SP	#127# 5-acetyl-7-chlorofuro[2,3-c]pyridine + NADH + H+ =
	5-(1-hydroxyethyl)-7-chlorofuro[2,3-c]pyridine + NAD+ {r} <225>
SP	#127# 5-acetylfuro[2,3-c]pyridine + NADH + H+ =
	5-(1-hydroxyethyl)furo[2,3-c]pyridine + NAD+ {r} <225>
SP	#127# acetoin + NADH + H+ = 3-hydroxy-2-butanol + NAD+ {r} <225>
SP	#127# acetone + NADH + H+ = 2-propanol + NAD+ <225>
SP	#127# acetylacetone + 2 NADH + 2 H+ = 2,4-pentanediol + 2 NAD+ {r} <225>
SP	#127# acetylpyrazine + NADH + H+ = (R)-1-(pyrazyl)ethanol + NAD+ {r}
	<225>
SP	#127# chloroacetone + NADH + H+ = 1-chloro-2-propanol + NAD+ {r} <225>
SP	#127# diacetyl + NADH + H+ = 2,3-butandiol + NAD+ {r} <225>
SP	#127# diethylketone + NADH + H+ = 3-pentanol + NAD+ {r} <225>
SP	#127# ethyl 4-chloroacetoacetate + NADH + H+ = ethyl
	4-chloro-3-hydroxybutanoate + NAD+ {r} <225>
SP	#127# ethyl acetoacetate + NADH + H+ = ethyl 3-hydroxybutanoate + NAD+
	{r} <225>
SP	#127# ethyl pyruvate + NADH + H+ = ethyl lactate + NAD+ {r} <225>
SP	#127# methyl acetoacetate + NADH + H+ = methyl 3-hydroxybutanoate +
	NAD+ {r} <225>
SP	#127# methyl pyruvate + NADH + H+ = methyl lactate + NAD+ {r} <225>
SP	#127# oxaloacetate + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# propionaldehyde + NADH + H+ = 1-propanol + NAD+ {r} <225>
SP	#127# pyridine 2-aldehyde + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# pyridine 3-aldehyde + NADH + H+ = ? + NAD+ {r} <225>
SP	#127# pyridine 4-aldehyde + NADH + H+ = ? + NAD+ {r} <225>
SP	#128,149# 2,3-butanediol + NAD+ = acetoin + NADH + H+ (#149# 272% of
	the activity with 1-phenylethanol <243>) <230,243>
SP	#128,149# 2,3-butanediol + NAD+ = acetoin + NADH + H+ (#149# 272% of
	the activity with 1-phenylethanol <243>) {r} <230,243>
SP	#13# secondary alcohol + NAD+ = aldehyde + NADH <126>
SP	#13# cinnamaldehyde + NADH + H+ = cinnamyl alcohol + NAD+ {r} <234>
SP	#13# cinnamyl alcohol + NAD+ = cinnamaldehyde + NADH + H+ {r} <234>
SP	#13# 2-propanol + NAD+ = aceton + NADH + H+ |#13# irreversible, no
	measurable activity with acetone <234>| {ir} <234>
SP	#13,111,154# propan-2-ol + NAD+ = acetone + NADH + H+ (#154# 65% of the
	activity with butan-1-ol <271>) |#111# 6% activity compared to
	cyclohexanone <197>; #13# synthesis of [4R-(2)H]NADH with high yield by
	enzymatic oxidation of 2-propanol-d(8) <269>| {r} <197,269,271>
SP	#13,111,154# propan-2-ol + NAD+ = acetone + NADH + H+ (#154# 65% of the
	activity with butan-1-ol <271>) |#111# 6% activity compared to
	cyclohexanone <197>; #13# synthesis of [4R-(2)H]NADH with high yield by
	enzymatic oxidation of 2-propanol-d(8) <269>| <197,269,271>
SP	#131# 2-decanone + NADH = (S)-2-decanol + NAD+ + H+ |#131# 92%
	enantiomeric excess <239>| <239>
SP	#131# 2-heptanone + NADH = (S)-2-heptanol + NAD+ + H+ |#131# 79%
	enantiomeric excess <239>| <239>
SP	#131# 2-hexanone + NADH = (S)-2-hexanol + NAD+ + H+ |#131# 37%
	enantiomeric excess <239>| <239>
SP	#131# 2-nonanone + NADH = (S)-2-nonanol + NAD+ + H+ |#131# 95%
	enantiomeric excess <239>| <239>
SP	#131# 2-octanone + NADH = (S)-2-octanol + NAD+ + H+ |#131# 92%
	enantiomeric excess <239>| <239>
SP	#131# 2-pentanone + NADH = (S)-2-pentanol + NAD+ + H+ |#131# 60%
	enantiomeric excess <239>| <239>
SP	#131# 4-methoxyphenylacetone + NADH =
	(2S)-1-(4-methoxyphenyl)propan-2-ol + NAD+ + H+ <239>
SP	#131# tert-butyl acetoacetate + NADH + H+ = ? <239>
SP	#132# 3-methylbutanal + NAD+ = ? + NADH + H+ (#132# about 10% of the
	activity with ethanol or 1-propanol <237>) <237>
SP	#132# butanol + NAD+ = 1-butanal + NADH + H+ (#132# about 15% of the
	activity with ethanol or 1-propanol <237>) <237>
SP	#132# pentanol + NAD+ = 1-pentanal + NADH + H+ (#132# about 10% of the
	activity with ethanol or 1-propanol <237>) <237>
SP	#142# acetoin + NAD+ = diacetyl + NADH (#142# 18% of the activity with
	2,3-butanediol <138>) <138>
SP	#142# diacetyl + NADH + H+ = acetoin + NAD+ (#142# 150% of the activity
	with acetoin <138>) <138>
SP	#142# dihydroxyacetone + NADH + H+ = glycerol + NAD+ (#142# 36% of the
	activity with acetoin <138>) <138>
SP	#142# acetoin + NADH + H+ = butan-2,3-diol + NAD+ <138>
SP	#142# butan-2,3-diol + NAD+ = acetoin + NADH + H+ <138>
SP	#142# D-arabinose + NADH + H+ = D-arabitol + NAD+ (#142# 66% of the
	activity with 2,3-butanediol <138>) <138>
SP	#142# dihydroxyacetone phosphate + NADH + H+ = glycerol phosphate +
	NAD+ (#142# 82% of the activity with acetoin <138>) <138>
SP	#142# DL-glyceraldehyde + H+ = glycerol + NAD+ (#142# 31% of the
	activity with acetoin <138>) <138>
SP	#142# hexanal + NADH + H+ = hexan-1-ol + NAD+ (#142# 16% of the
	activity with acetoin <138>) <138>
SP	#142# pyruvaldehyde + NADH + H+ = lactaldehyde + NAD+ (#142# 81% of the
	activity with acetoin <138>) <138>
SP	#149# acetoin + NADH + H+ = 2,3-butanediol + NAD+ {r} <243>
SP	#149# 2,2,2-trifluoroacetophenone + NADPH + H+ =
	(R)-2,2,2-trifluoro-1-phenylethanol + NADP+ (#149# 180% of the activity
	with acetoin <243>) {r} <243>
SP	#149# 1-(3-bromophenyl)ethanol + NAD+ = 1-(3-bromophenyl)ethanone +
	NADH + H+ (#149# 315% of the activity with 1-phenylethanol <243>) <243>
SP	#149# 1-(3-chlorophenyl)ethanol + NAD+ = 1-(3-chlorophenyl)ethanone +
	NADH + H+ (#149# 205% of the activity with 1-phenylethanol <243>) <243>
SP	#149# 1-(4-bromophenyl)ethanol + NAD+ = 1-(4-bromophenyl)ethanone +
	NADH + H+ (#149# 167% of the activity with 1-phenylethanol <243>) <243>
SP	#149# 1-(4-chlorophenyl)ethanol + NAD+ = 1-(4-chlorophenyl)ethanone +
	NADH + H+ (#149# 151% of the activity with 1-phenylethanol <243>) <243>
SP	#149# 1-(4-methylphenyl)ethanol + NAD+ = 1-(4-methylphenyl)ethanone +
	NADH + H+ (#149# 189% of the activity with 1-phenylethanol <243>) <243>
SP	#149# 1-phenylethanol + NADP+ = 1-phenylethanone + NADPH + H+ <243>
SP	#149# 2-heptanol + NAD+ = heptan-2-one + NADH + H+ (#149# 62% of the
	activity with 1-phenylethanol <243>) <243>
SP	#149# 2-oxopropanal + NADH + H+ = ? + NAD+ (#149# 328% of the activity
	with acetoin <243>) {r} <243>
SP	#149# ethyl 2-oxopropanoate + NADPH + H+ = (R)-ethyl
	2-hydroxypropanoate + NADP+ (#149# 294& of the activity with acetoin
	<243>) {r} <243>
SP	#15#
	(6S)-5,6-dihydro-6-methyl-4H-thieno[2,3b]thiopyran-4-one-7,7-dioxide +
	NADH + H+ =
	(4S,6S)-5,6-dihydro-4-hydroxy-6-methyl-4H-thieno[2,3b]thiopyran-7
	7-dioxide + NAD+ {} <134>
SP	#150# benzaldehyde + NADPH + H+ = benzyl alcohol + NADP+ (#150# 107% of
	the activity with (2E)-but-2-enal, yield 99% after 12 h <244>) {r} <244>
SP	#150# benzyl alcohol + NADP+ = benzaldehyde + NADPH + H+ {r} <244>
SP	#150# (2E)-2-methylpent-2-enal + NADPH + H+ =
	(2E)-2-methylpent-2-en-1-ol + NADP+ (#150# 41.5% of the activity with
	(2E)-but-2-enal, yield 95% after 12 h <244>) <244>
SP	#150# (2E)-3,7-dimethylocta-2,6-dienal + NADPH + H+ =
	(2E)-3,7-dimethylocta-2,6-dien-1-ol + NADP+ (#150# 37.4% of the
	activity with (2E)-but-2-enal, yield 87% after 12 h <244>) <244>
SP	#150# (2E)-but-2-en-1-ol + NADP+ = (2E)-but-2-enal + NADPH + H+ {r}
	<244>
SP	#150# (2E)-but-2-enal + NADPH + H+ = (2E)-but-2-en-1-ol + NADP+ (#150#
	yield 96% after 12 h <244>) {r} <244>
SP	#150# (2E)-dec-2-enal + NADPH + H+ = (2E)-dec-2-en-1-ol + NADP+ (#150#
	16.7% of the activity with (2E)-but-2-enal, yield 91% after 12 h <244>)
	<244>
SP	#150# (2E)-hex-2-enal + NADPH + H+ = (2E)-hex-2-en-1-ol + NADP+ (#150#
	41.7% of the activity with (2E)-but-2-enal, yield 98% after 12 h <244>)
	<244>
SP	#150# (2E)-oct-2-enal + NADPH + H+ = (2E)-oct-2-en-1-ol + NADP+ (#150#
	30.2% of the activity with (2E)-but-2-enal, yield 69% after 12 h <244>)
	|#150# plus 27% oct-2-enyl ester <244>| <244>
SP	#152# all-trans retinal + NADH + H+ = all-trans retinol + NAD+ (#152#
	26.8% of the activity with butan-1-ol <272>) <272>
SP	#152# hexan-1-ol + NAD+ = hexanal + NADH + H+ (#152# 77.1% of the
	activity with butan-1-ol <272>) <272>
SP	#153# 2,2,2-trifluoro-1-phenylethanone + propan-2-ol =
	(1R)-2,2,2-trifluoro-1-phenylethanol + acetone (#153# in presence of
	propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed
	without addition of NADH <280>) |#153# 99% conversion, 99% enantiomeric
	excess <280>| <280>
SP	#153# 2,2-difluoro-1-phenylethanone + propan-2-ol =
	(1R)-2,2-difluoro-1-phenylethanol + acetone (#153# in presence of
	propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed
	without addition of NADH <280>) |#153# 99% conversion, 94% enantiomeric
	excess <280>| <280>
SP	#153# 2-fluoro-1-(4-chlorophenyl)ethanone + propan-2-ol =
	(1R)-2-fluoro-1-(4-chlorophenyl)ethanol + acetone (#153# in presence of
	propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed
	without addition of NADH <280>) |#153# 99% conversion, 98% enantiomeric
	excess <280>| <280>
SP	#153# 2-fluoro-1-(4-fluorophenyl)ethanone + propan-2-ol =
	(1R)-2-fluoro-1-(4-fluorophenyl)ethanol + acetone (#153# in presence of
	propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed
	without addition of NADH <280>) |#153# 99% conversion, 97% enantiomeric
	excess <280>| <280>
SP	#153# 2-fluoro-1-(4-iodophenyl)ethanone + propan-2-ol =
	(1R)-2-fluoro-1-(4-iodophenyl)ethanol + acetone (#153# in presence of
	propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed
	without addition of NADH <280>) |#153# 99% conversion, 99% enantiomeric
	excess <280>| <280>
SP	#153# 2-fluoro-1-phenylethanone + propan-2-ol =
	(1R)-2-fluoro-1-phenylethanol + acetone (#153# in presence of
	propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed
	without addition of NADH <280>) |#153# 99% conversion, 99% enantiomeric
	excess <280>| <280>
SP	#154# 1,5-pentanediol + NAD+ = ? + NADH + H+ (#154# 18% of the activity
	with butan-1-ol <271>) <271>
SP	#154# butanal + NADH + H+ = butan-1-ol + NAD+ {r} <271>
SP	#18# 3-butene-1-ol + NAD+ = ? + NADH <75>
SP	#18# 3-phenyl-2-propen-1-ol + NAD+ = ? + NADH <75>
SP	#18,35,37,66,77,80# hexan-1-ol + NAD+ = n-hexanal + NADH
	<47,61,75,77,78,85,97>
SP	#18,66,69,77,80# 2-methylpropan-1-ol + NAD+ = 2-methyl-propan-1-one +
	NADH (#18# weak activity <75>) <61,75,77,78,84,97>
SP	#18,66,69,77,80# 2-methylpropan-1-ol + NAD+ = 2-methyl-propan-1-one +
	NADH (#18# weak activity <75>) {} <61,75,77,78,84,97>
SP	#20# isopentan-1-ol + NAD+ = isopentanal + NADH + H+ (#20# 34% of the
	activity with ethanol <284>) <284>
SP	#20,118# pentan-1-ol + NAD+ = pentanal + NADH + H+ (#20# 75.6% of the
	activity with ethanol <284>) |#118# 76% of the activity with butan-2-ol
	<256>| <256,284>
SP	#20,118,139,152,154# propan-1-ol + NAD+ = propanal + NADH + H+ (#154#
	55% of the activity with butan-1-ol <271>; #152# 64.3% of the activity
	with butan-1-ol <272>; #20# 89.3% of the activity with ethanol <284>)
	|#118# 68% of the activity with butan-2-ol <256>| <254,256,271,272,284>
SP	#20,118,139,152,154# propan-1-ol + NAD+ = propanal + NADH + H+ (#154#
	55% of the activity with butan-1-ol <271>; #152# 64.3% of the activity
	with butan-1-ol <272>; #20# 89.3% of the activity with ethanol <284>)
	|#118# 68% of the activity with butan-2-ol <256>| {r}
	<254,256,271,272,284>
SP	#20,152,154# butan-1-ol + NAD+ = butanal + NADH + H+ (#154# best
	substrate <271>; #20# 90.7% of the activity with ethanol <284>)
	<271,272,284>
SP	#20,152,154# butan-1-ol + NAD+ = butanal + NADH + H+ (#154# best
	substrate <271>; #20# 90.7% of the activity with ethanol <284>) {r}
	<271,272,284>
SP	#21# methylglyoxal + NADH = ? + NADH (#21# 11.9% of the activity with
	acetaldehyde <72>) <72>
SP	#21# 2,3-pentanedione + NADH = ? + NADH (#21# 5.5% of the activity with
	acetaldehyde <72>) <72>
SP	#21,40,41,54# propionaldehyde + NADH = propanol + NAD+ (#21# 94% of the
	activity with acetaldehyde <72>) <42,68,72,99>
SP	#24# acetophenone + NADH = (R)-alpha-phenyl ethanol + NAD+ (#24# the
	enzyme exhibits high stereoselectivity in the desymmetrization of the
	prochiral ketone acetophenone, producing optically pure
	(R)-alpha-phenyl ethanol at high conversion <106>) <106>
SP	#24,40# cyclohexanone + NADH = cyclohexanol + NAD+ (#24# best cyclic
	ketone substrate <106>) <28,42,106>
SP	#25# diacetyl + NADH + H+ = ? (#25# 16.1fold higher activity compared
	to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 1-octanol + NAD+ = 1-octanal + NADH + H+ (#25# 6% of activity with
	N-benzyl-3-pyrrolidinol <188>) <188>
SP	#25# 2-acetylpyrrole + NADH + H+ = 1-(1H-pyrrol-2-yl)ethanol + NAD+
	(#25# 70% of activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 2-butanone + NADH + H+ = butan-2-ol + NAD+ (#25# 2.8fold higher
	activity compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 2-hexanone + NADH + H+ = hexan-2-ol + NAD+ (#25# 50.4fold higher
	activity compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 2-nitrobenzaldehyde + NADH + H+ = (2-nitrophenyl)methanol + NAD+
	(#25# 33% of activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 2-oxo-butyric acid + NADH + H+ = 2-hydroxybutyric acid + NAD+
	(#25# 15% of activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 3-acetylpyridine + NADH + H+ = 1-pyridin-3-ylethanol + NAD+ (#25#
	7.9fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 3-phenylpropionaldehyde + NADH + H+ = 3-phenylpropanol + NAD+
	(#25# 6.9fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# 4-acetylpyridine + NADH + H+ = 1-pyridin-4-ylethanol + NAD+ (#25#
	64.5fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# acetone + NADH + H+ = propan-2-ol + NAD+ (#25# 1.9fold higher
	activity compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# benzoin + NADH + H+ = 1,2-diphenylethane-1,2-diol (#25# 13% of
	activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# benzyloxycarbonyl-3-pyrrolidinone + NADH + H+ =
	(S)-benzyloxycarbonyl-3-pyrrolidinol + NAD+ (#25# production with 99.6%
	enantiomeric excess <188>) <188>
SP	#25# dihydro-4,4-dimethyl-2,3-furandione + NADH + H+ = ? (#25# 13.1fold
	higher activity compared to activity with N-benzyl-3-pyrrolidinone
	<188>) <188>
SP	#25# ethyl 4-chloroacetoacetate + NADH + H+ = ? (#25# 6.8fold higher
	activity compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# ethyl acetoacetate + NADH + H+ = ? (#25# 42.4fold higher activity
	compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# glutaraldehyde + NADH + H+ = ? (#25# 70.8fold higher activity
	compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# hexanal + NADH + H+ = n-hexanol + NAD+ (#25# 22.3fold higher
	activity compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# levulinic acid + NADH + H+ = ? (#25# 11% of activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# m-chlorophenacyl chloride + NADH + H+ =
	2-chloro-1-(3-chlorophenyl)ethanol + NAD+ (#25# 4.6fold higher activity
	compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# methyl glyoxal + NADH + H+ = ? (#25# 3.5fold higher activity
	compared to activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# methyl pyruvate + NADH + H+ = methyl 2-hydroxypropanoate + NAD+
	(#25# 18.9fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# N-benzyl-3-piperidone + NADH + H+ = N-benzylpiperidin-3-ol + NAD+
	(#25# 2.3fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# N-benzyl-3-pyrrolidinone + NADH + H+ = (R)-N-benzyl-3-pyrrolidinol
	+ NAD+ (#25# (R)-stereoselectivity of the reduction carried out with
	the heat-treated cells <188>) {r} <188>
SP	#25# N-benzyl-4-piperidone + NADH + H+ = N-benzylpiperidin-4-ol + NAD+
	(#25# 10.7fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# n-butyraldehyde + NADH + H+ = n-butanol + NAD+ (#25# 7.3fold
	higher activity compared to activity with N-benzyl-3-pyrrolidinone
	<188>) <188>
SP	#25# N-tert-butoxycarbonyl-3-pyrrolidinone + NADH + H+ =
	(S)-N-tert-butoxycarbonyl-3-pyrrolidinol + NAD+ (#25# production of
	(S)-N-tert-butoxycarbonyl-3-pyrrolidinol with 99.6% enantiomeric excess
	<188>) <188>
SP	#25# oxalacetic acid + NADH + H+ = ? (#25# 14% of activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# p-chlorobenzaldehyde + NADH + H+ = p-chlorobenzyl alcohol + NAD+
	(#25# 1.2fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# p-nitrobenzyloxycarbonyl-3-pyrrolidinone + NADH + H+ =
	(S)-N-p-nitrobenzyloxycarbonyl-3-pyrrolidinol + NAD+ (#25# production
	with 90.7% enantiomeric excess <188>) <188>
SP	#25# phenylethanol + NAD+ = phenylacetaldehyde + NADH + H+ (#25# 15% of
	activity with N-benzyl-3-pyrrolidinol <188>) <188>
SP	#25# propiophenone + NADH + H+ = 1-phenylpropan-1-ol + NAD+ (#25# 27%
	of activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# pyridine-3-aldehyde + NADH + H+ = pyridin-3-yl ethanol + NAD+
	(#25# 82% of activity with N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25# pyridine-4-aldehyde + NADH + H+ = pyridin-4-yl methanol + NAD+
	(#25# 4.4fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <188>
SP	#25,100# N-benzyl-3-pyrrolidinone + NADH + H+ =
	(S)-N-benzyl-3-pyrrolidinol + NAD+ (#100# (S)-N-benzyl-3-pyrrolidinol
	is produced at an enantiomeric excess of more than 99.9% <185>) {r}
	<185,188>
SP	#25,43,100,123,127# acetophenone + NADH + H+ = 1-phenylethanol + NAD+
	(#25# 1.8fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>; #100# 40% of the activity with
	N-benzyl-3-pyrrolidinone <185>) {r} <185,188,218,225,232>
SP	#25,43,100,123,127# acetophenone + NADH + H+ = 1-phenylethanol + NAD+
	(#25# 1.8fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>; #100# 40% of the activity with
	N-benzyl-3-pyrrolidinone <185>) <185,188,218,225,232>
SP	#25,91,100,110,126,131# 2-pentanol + NAD+ = 2-pentanone + NADH + H+
	(#91# weak activity <144>; #126# low activity <222>; #25# 45% of
	activity with N-benzyl-3-pyrrolidinol <188>; #100# activity is 9fold
	higher than with (S)-N-benzyl-3-pyrrolidinol <185>; #110# 5.7% activity
	compared to ethanol <213>) <144,185,188,213,222,239>
SP	#25,91,100,110,126,131# 2-pentanol + NAD+ = 2-pentanone + NADH + H+
	(#91# weak activity <144>; #126# low activity <222>; #25# 45% of
	activity with N-benzyl-3-pyrrolidinol <188>; #100# activity is 9fold
	higher than with (S)-N-benzyl-3-pyrrolidinol <185>; #110# 5.7% activity
	compared to ethanol <213>) {r} <144,185,188,213,222,239>
SP	#25,92# 1-phenyl-2-butanone + NADH + H+ = 1-phenylbutan-2-ol + NAD+
	(#92# 12% of the activity with phenyl trifluoromethyl ketone <137>;
	#25# 1.5fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <137,188>
SP	#25,92# chloroacetone + NADH + H+ = 1-chloropropan-2-ol + NAD+ (#92#
	238% of the activity with phenyl trifluoromethyl ketone <137>; #25#
	41.7fold higher activity compared to activity with
	N-benzyl-3-pyrrolidinone <188>) <137,188>
SP	#26# ethylene glycol + NAD+ = ? (#26# poor substrate <129>) {r} <129>
SP	#26# primary or secondary alcohol + NAD+ = aldehyde or ketone + NADH
	{r} <129>
SP	#28# 6-benzyloxy-3,5-dioxo-hexanoic acid ethyl ester + NADH + H+ =
	(3R,5S)-6-benzyloxy-3,5-dihydroxy-hexanoic acid ethyl ester + NAD+ {}
	<133>
SP	#3,10,18,37,41,81# allyl alcohol + NAD+ = prop-2-en-1-al + NADH (#10#
	no activity <87>) <4,67,68,75,83,85,87,97>
SP	#3,10,18,37,41,81# allyl alcohol + NAD+ = prop-2-en-1-al + NADH (#10#
	no activity <87>) {} <4,67,68,75,83,85,87,97>
SP	#3,4,5,9,10,14,23,40,41,42,44,47,51,53,54,59,69,113,118,126,127,135,136
	137,143,146,152,155,156# acetaldehyde + NADH + H+ = ethanol + NAD+
	(#126# best substrate <222>; #54# the reduction of acetaldehyde is
	4.9fold faster than the oxidation of ethanol <99>; #5# reduced by
	isoenzyme A2 and C2, no activity with isoenzyme B2 <48>; #3# reduced at
	the highest rate of all aldehydes tested <4>; #10# cells with an extra
	copy of ADH1 display chronological life-span extension. Antioxidant
	enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1
	copy show extended replicative life span and increased Sir2p activity
	<190>; #10# mutant enzyme S109P/L116S/Y294C <193>; #152# 83.2% of the
	activity with butan-1-ol <272>; #155,156# AdhE is a bifunctional
	enzyme, containing both aldehyde dehydrogenase and alcohol
	dehydrogenase activities <281>) |#118# 100% of the activity with
	butan-2-ol <256>| {r}
	<4,6,25,28,41,42,43,48,49,51,68,81,82,84,90,99,123,146,151,190,193,215
	222,223,225,246,252,256,259,265,272,281,282>
SP	#3,4,5,9,10,14,23,40,41,42,44,47,51,53,54,59,69,113,118,126,127,135,136
	137,143,146,152,155,156# acetaldehyde + NADH + H+ = ethanol + NAD+
	(#126# best substrate <222>; #54# the reduction of acetaldehyde is
	4.9fold faster than the oxidation of ethanol <99>; #5# reduced by
	isoenzyme A2 and C2, no activity with isoenzyme B2 <48>; #3# reduced at
	the highest rate of all aldehydes tested <4>; #10# cells with an extra
	copy of ADH1 display chronological life-span extension. Antioxidant
	enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1
	copy show extended replicative life span and increased Sir2p activity
	<190>; #10# mutant enzyme S109P/L116S/Y294C <193>; #152# 83.2% of the
	activity with butan-1-ol <272>; #155,156# AdhE is a bifunctional
	enzyme, containing both aldehyde dehydrogenase and alcohol
	dehydrogenase activities <281>) |#118# 100% of the activity with
	butan-2-ol <256>| {}
	<4,6,25,28,41,42,43,48,49,51,68,81,82,84,90,99,123,146,151,190,193,215
	222,223,225,246,252,256,259,265,272,281,282>
SP	#3,4,5,9,10,14,23,40,41,42,44,47,51,53,54,59,69,113,118,126,127,135,136
	137,143,146,152,155,156# acetaldehyde + NADH + H+ = ethanol + NAD+
	(#126# best substrate <222>; #54# the reduction of acetaldehyde is
	4.9fold faster than the oxidation of ethanol <99>; #5# reduced by
	isoenzyme A2 and C2, no activity with isoenzyme B2 <48>; #3# reduced at
	the highest rate of all aldehydes tested <4>; #10# cells with an extra
	copy of ADH1 display chronological life-span extension. Antioxidant
	enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1
	copy show extended replicative life span and increased Sir2p activity
	<190>; #10# mutant enzyme S109P/L116S/Y294C <193>; #152# 83.2% of the
	activity with butan-1-ol <272>; #155,156# AdhE is a bifunctional
	enzyme, containing both aldehyde dehydrogenase and alcohol
	dehydrogenase activities <281>) |#118# 100% of the activity with
	butan-2-ol <256>|
	<4,6,25,28,41,42,43,48,49,51,68,81,82,84,90,99,123,146,151,190,193,215
	222,223,225,246,252,256,259,265,272,281,282>
SP	#31# prop-2-en-1-ol + NAD+ = ? + NADH (#31# 140.6% of the activity with
	ethanol <73>) <73>
SP	#31# (Z)-hex-2-en-1-ol + NAD+ = (Z)-hex-2-en-1-one + NADH (#31# 9.7% of
	the activity with ethanol <73>) <73>
SP	#35# methylcrotonyl alcohol + NAD+ = methylcrotonaldehyde + NADH <95>
SP	#37,40,45,69,77# pentan-2-ol + NAD+ = 2-pentanone + NADH (#40#
	(R)-2-pentanol and (S)-2-pentanol <31>) <31,61,66,84,85>
SP	#37,40,45,69,77# pentan-2-ol + NAD+ = 2-pentanone + NADH (#40#
	(R)-2-pentanol and (S)-2-pentanol <31>) {r} <31,61,66,84,85>
SP	#37,40,81# cinnamyl alcohol + NAD+ = cinnamaldehyde + NADH <83,85,92>
SP	#39# 1-phenyl-2-propanone + NADH + H+ = (S)-1-phenyl-2-propanol + NAD+
	{} <131>
SP	#4,5,7,8,9,10,12,13,14,18,19,21,23,26,27,30,31,33,35,40,41,42,44,46,49
	51,52,54,57,60,65,66,67,68,69,70,71,72,74,78,79,80,81,82,87,89,97#
	ethanol + NAD+ = acetaldehyde + NADH (#87# best substrate <118>; #8#
	class III isoenzyme chi-ADH oxidizes ethanol very poorly <16>; #8# no
	oxidation with class III enzyme <11>; #9# isoenzyme ADH-1 and ADH-3, no
	activity with isoenzyme ADH-2 <49>; #54# the reduction of acetaldehyde
	is 4.9fold faster than the oxidation of ethanol <99>; #51# the
	reduction of acetaldehyde of ADH-MII is about 7times higher than that
	of the oxidation of ethanol <82>; #5# no activity with isoenzyme B2,
	oxidized by isoenzyme A2 and C2 <48>; #5# role of the major liver
	isoenzyme A2 in ethanol metabolism <48>; #40# plays an important role
	in the metabolism of ethanol <102>; #8# chi-ADH plays an important role
	in the metabolism of long chain alcohols and aldehydes <21>; #8# the
	anodic enzyme form may contribute significantly to alcohol elimination
	in man, particularly at high concentrations when the other enzyme
	species are saturated <18>; #8# the enzyme plays a significant role in
	first-pass metabolism of ethanol in human <96>; #8# enzyme is
	responsible for the major ethanol oxidation capacity in the body. The
	products acetaldehyde and NADH are responsible for the most of the
	toxic effects and metabolic disturbances produced by ethanol ingestion
	<10>; #10# rate-limiting step of the alcoholic fermentation <122>; #40#
	isomerization of the enzyme-NAD+ complex is the rate-limiting step for
	acetaldehyde reduction by the wild-type enzyme <111>; #89# no
	cooperativity between the 2 active sites of the enzyme <105>; #5# DH3
	plays an important role in systemic ethanol metabolism at higher levels
	of blood ethanol through activation by cytoplasmic solution
	hydrophobicity <141>; #46# 76% of the activity with 2-phenylethanol
	<149>; #13# proton and hydride equivalent transfer in the alcohol
	dehydrogenase enzymatic reaction are modulated by the correlated
	motions between NAD+ and the cofactor domain <176>) |#60# acetaldehyde
	is the best substrate for isozyme ADH I <113>| {}
	<2,6,10,11,12,13,14,16,17,18,20,21,24,25,28,35,41,42,43,45,47,48,49,51
	52,53,59,60,64,65,67,68,69,71,72,73,74,75,76,77,78,81,82,83,84,87,90,92
	95,96,97,99,101,102,105,111,113,115,116,117,118,119,120,121,122,126,128
	135,141,147,149,170,172,176,181>
SP	#4,5,7,8,9,10,12,13,14,18,19,21,23,26,27,30,31,33,35,40,41,42,44,46,49
	51,52,54,57,60,65,66,67,68,69,70,71,72,74,78,79,80,81,82,87,89,97#
	ethanol + NAD+ = acetaldehyde + NADH (#87# best substrate <118>; #8#
	class III isoenzyme chi-ADH oxidizes ethanol very poorly <16>; #8# no
	oxidation with class III enzyme <11>; #9# isoenzyme ADH-1 and ADH-3, no
	activity with isoenzyme ADH-2 <49>; #54# the reduction of acetaldehyde
	is 4.9fold faster than the oxidation of ethanol <99>; #51# the
	reduction of acetaldehyde of ADH-MII is about 7times higher than that
	of the oxidation of ethanol <82>; #5# no activity with isoenzyme B2,
	oxidized by isoenzyme A2 and C2 <48>; #5# role of the major liver
	isoenzyme A2 in ethanol metabolism <48>; #40# plays an important role
	in the metabolism of ethanol <102>; #8# chi-ADH plays an important role
	in the metabolism of long chain alcohols and aldehydes <21>; #8# the
	anodic enzyme form may contribute significantly to alcohol elimination
	in man, particularly at high concentrations when the other enzyme
	species are saturated <18>; #8# the enzyme plays a significant role in
	first-pass metabolism of ethanol in human <96>; #8# enzyme is
	responsible for the major ethanol oxidation capacity in the body. The
	products acetaldehyde and NADH are responsible for the most of the
	toxic effects and metabolic disturbances produced by ethanol ingestion
	<10>; #10# rate-limiting step of the alcoholic fermentation <122>; #40#
	isomerization of the enzyme-NAD+ complex is the rate-limiting step for
	acetaldehyde reduction by the wild-type enzyme <111>; #89# no
	cooperativity between the 2 active sites of the enzyme <105>; #5# DH3
	plays an important role in systemic ethanol metabolism at higher levels
	of blood ethanol through activation by cytoplasmic solution
	hydrophobicity <141>; #46# 76% of the activity with 2-phenylethanol
	<149>; #13# proton and hydride equivalent transfer in the alcohol
	dehydrogenase enzymatic reaction are modulated by the correlated
	motions between NAD+ and the cofactor domain <176>) |#60# acetaldehyde
	is the best substrate for isozyme ADH I <113>| {r}
	<2,6,10,11,12,13,14,16,17,18,20,21,24,25,28,35,41,42,43,45,47,48,49,51
	52,53,59,60,64,65,67,68,69,71,72,73,74,75,76,77,78,81,82,83,84,87,90,92
	95,96,97,99,101,102,105,111,113,115,116,117,118,119,120,121,122,126,128
	135,141,147,149,170,172,176,181>
SP	#4,5,7,8,9,10,12,13,14,18,19,21,23,26,27,30,31,33,35,40,41,42,44,46,49
	51,52,54,57,60,65,66,67,68,69,70,71,72,74,78,79,80,81,82,87,89,97#
	ethanol + NAD+ = acetaldehyde + NADH (#87# best substrate <118>; #8#
	class III isoenzyme chi-ADH oxidizes ethanol very poorly <16>; #8# no
	oxidation with class III enzyme <11>; #9# isoenzyme ADH-1 and ADH-3, no
	activity with isoenzyme ADH-2 <49>; #54# the reduction of acetaldehyde
	is 4.9fold faster than the oxidation of ethanol <99>; #51# the
	reduction of acetaldehyde of ADH-MII is about 7times higher than that
	of the oxidation of ethanol <82>; #5# no activity with isoenzyme B2,
	oxidized by isoenzyme A2 and C2 <48>; #5# role of the major liver
	isoenzyme A2 in ethanol metabolism <48>; #40# plays an important role
	in the metabolism of ethanol <102>; #8# chi-ADH plays an important role
	in the metabolism of long chain alcohols and aldehydes <21>; #8# the
	anodic enzyme form may contribute significantly to alcohol elimination
	in man, particularly at high concentrations when the other enzyme
	species are saturated <18>; #8# the enzyme plays a significant role in
	first-pass metabolism of ethanol in human <96>; #8# enzyme is
	responsible for the major ethanol oxidation capacity in the body. The
	products acetaldehyde and NADH are responsible for the most of the
	toxic effects and metabolic disturbances produced by ethanol ingestion
	<10>; #10# rate-limiting step of the alcoholic fermentation <122>; #40#
	isomerization of the enzyme-NAD+ complex is the rate-limiting step for
	acetaldehyde reduction by the wild-type enzyme <111>; #89# no
	cooperativity between the 2 active sites of the enzyme <105>; #5# DH3
	plays an important role in systemic ethanol metabolism at higher levels
	of blood ethanol through activation by cytoplasmic solution
	hydrophobicity <141>; #46# 76% of the activity with 2-phenylethanol
	<149>; #13# proton and hydride equivalent transfer in the alcohol
	dehydrogenase enzymatic reaction are modulated by the correlated
	motions between NAD+ and the cofactor domain <176>) |#60# acetaldehyde
	is the best substrate for isozyme ADH I <113>|
	<2,6,10,11,12,13,14,16,17,18,20,21,24,25,28,35,41,42,43,45,47,48,49,51
	52,53,59,60,64,65,67,68,69,71,72,73,74,75,76,77,78,81,82,83,84,87,90,92
	95,96,97,99,101,102,105,111,113,115,116,117,118,119,120,121,122,126,128
	135,141,147,149,170,172,176,181>
SP	#4,8,10,12,14,18,37,40,41,45,54,69,71,74,77# propan-2-ol + NAD+ =
	acetone + NADH (#10# no activity <87>; #41# very low activity <67>;
	#54# 3% of the activity with ethanol <99>)
	<14,43,45,61,64,65,66,67,68,81,84,85,87,90,92,97,99>
SP	#4,8,10,12,14,18,37,40,41,45,54,69,71,74,77# propan-2-ol + NAD+ =
	acetone + NADH (#10# no activity <87>; #41# very low activity <67>;
	#54# 3% of the activity with ethanol <99>) {}
	<14,43,45,61,64,65,66,67,68,81,84,85,87,90,92,97,99>
SP	#4,8,10,12,18,19,37,41,45,52,54,66,69,77,80,81# propanol + NADH =
	propionaldehyde + NADH
	<20,45,53,59,61,65,66,67,68,71,75,77,78,83,84,85,87,90,96,97,99>
SP	#4,8,10,12,18,19,37,41,45,52,54,66,69,77,80,81# propanol + NADH =
	propionaldehyde + NADH {}
	<20,45,53,59,61,65,66,67,68,71,75,77,78,83,84,85,87,90,96,97,99>
SP	#4,8,18,35,37,40,45,52,69,71,74,77,81# butan-2-ol + NAD+ = butan-2-one
	+ NADH (#18# no activity <97>; #18# weak activity <75>; #40#
	(R)-2-butanol and (S)-2-butanol <31>)
	<20,31,47,53,59,61,64,66,75,83,84,85,92,95,97>
SP	#4,8,18,35,37,40,45,52,69,71,74,77,81# butan-2-ol + NAD+ = butan-2-one
	+ NADH (#18# no activity <97>; #18# weak activity <75>; #40#
	(R)-2-butanol and (S)-2-butanol <31>) {}
	<20,31,47,53,59,61,64,66,75,83,84,85,92,95,97>
SP	#4,8,9,10,12,18,35,37,40,41,45,52,66,68,71,74,77,80,81,82# butanol +
	NAD+ = butyraldehyde + NADH (#10# weak <87>; #41# activity with ADH I,
	no activity with ADH II <68>; #41# oxidized by enzyme form ADH-I, no
	activity with enzyme form ADH-II <67>; #9# pH 10.0: oxidized by ADH-1
	and ADH-3, no activity with isoenzyme ADH-2 <49>)
	<16,18,20,42,45,47,49,53,59,60,61,64,66,67,68,75,77,78,83,85,87,90,95
	96,97,101>
SP	#4,8,9,10,12,18,35,37,40,41,45,52,66,68,71,74,77,80,81,82# butanol +
	NAD+ = butyraldehyde + NADH (#10# weak <87>; #41# activity with ADH I,
	no activity with ADH II <68>; #41# oxidized by enzyme form ADH-I, no
	activity with enzyme form ADH-II <67>; #9# pH 10.0: oxidized by ADH-1
	and ADH-3, no activity with isoenzyme ADH-2 <49>) {}
	<16,18,20,42,45,47,49,53,59,60,61,64,66,67,68,75,77,78,83,85,87,90,95
	96,97,101>
SP	#40# ethanol + 3-benzoylpyridine-adenine dinucleotide = acetaldehyde +
	? (#40# rapid equilibrium bi bi mechanism <33>) {} <33>
SP	#40# 3-methyl-1-butanol + NAD+ = ? + NADH <92>
SP	#40# 3-pentanone + NADH = pentan-3-ol + NAD+ {r} <31>
SP	#40# 2-pentanone + NADH = pentan-2-ol + NAD+ {r} <31>
SP	#40# 3beta,17beta-dihydroxy-5beta-androstane + NAD+ =
	5beta-androstan-3,17dione + NADH <28>
SP	#40# 3beta-hydroxy-5beta-cholanoate + NAD+ = 3-oxo-5beta-cholanoate +
	NADH <28>
SP	#40# 3beta-hxdroxy-5alpha-cholanoate + NAD+ = 3-oxo-5alpha-cholanoate +
	NADH <28>
SP	#40# 5beta-pregnan-21-ol-3,20-dione hemisuccinate + NADH =
	5beta-pregnan-3,20,21-trione hemisuccinate + NADH <42>
SP	#40# all-trans-retinal + NADH + H+ = all-trans-retinol + NAD+ <93>
SP	#40# 11-cis-retinal + NADH + H+ = 11-cis-retinol + NAD+ <29>
SP	#40# 13-cis-retinal + NADH + H+ = 13-cis-retinol + NAD+ <29>
SP	#40# p-nitrophenyl octanoate + H2O = p-nitrophenol + octanoate (#40#
	acid-assisted nucleophilic catalysis involving the ammonium ion of Lys
	and the thiolate of Cys in the acyl-oxygen cleavage <39>) <39>
SP	#40# 5beta-cholanic acid-3-one + NAD+ = 5beta-cholanic acid-3-ol + NAD+
	<116>
SP	#40# butanol + NAD+ = n-butanal + NADH <111>
SP	#40# hexadecanol + NAD+ = hexadecanal + NADH + H+ (#40# immobilized
	HLAD shows about 60% reaction rate and free HLAD shows about 15%
	reaction rate with hexadecanol compared to ethanol at pH 8.8 and 30°C
	<204>) <204>
SP	#40# docosanol + NAD+ = ? + NADH + H+ (#40# immobilized HLAD shows
	about 60% reaction rate and free HLAD shows about 20% reaction rate
	with docosanol compared to ethanol at pH 8.8 and 30°C <204>) <204>
SP	#40# dodecanol + NAD+ = dodecanal + NADH + H+ (#40# immobilized HLAD
	shows about 60% reaction rate and free HLAD shows about 35% reaction
	rate with dodecanol compared to ethanol at pH 8.8 and 30°C <204>) <204>
SP	#40# ethanol + NAD+ = aldehyde + NADH + H+ (#40# immobilized HLAD shows
	100% reaction rate and free HLAD shows about 55% reaction rate with
	ethanol at pH 8.8 and 30°C <204>) <204>
SP	#40# tetracosanol + NAD+ = ? + NADH + H+ (#40# immobilized HLAD shows
	about 55% reaction rate and free HLAD shows about 15% reaction rate
	with tetracosanol compared to ethanol at pH 8.8 and 30°C <204>) <204>
SP	#40# benzyl alcohol + NAD+ = benzaldehyde + acycloNADH + H+ (#40#
	acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety
	has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
	<275>) <275>
SP	#40# butan-1-ol + NAD+ = butanal + acycloNADH + H+ (#40# acycloNAD+
	i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been
	replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety <275>) <275>
SP	#40# ethanol + acycloNAD+ = acetaldehyde + acycloNADH + H+ (#40#
	acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moietyhas
	been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety <275>)
	<275>
SP	#40# ethanol + NAD+ = acetaldehye + NADH + H+ <277>
SP	#40# hexan-1-ol + NAD+ = hexanal + acycloNADH + H+ (#40# acycloNAD+
	i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been
	replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety <275>) <275>
SP	#40# propan-1-ol + NAD+ = propanal + acycloNADH + H+ (#40# acycloNAD+
	i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been
	replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety <275>) <275>
SP	#40,111# butanol + NAD+ = butyraldehyde + NADH + H+ (#40# immobilized
	HLAD shows about 95% reaction rate and free HLAD shows about 90%
	reaction rate with butanol compared to ethanol at pH 8.8 and 30°C
	<204>) |#111# 359% activity compared to cyclohexanone <197>| {r}
	<197,204>
SP	#40,111# butanol + NAD+ = butyraldehyde + NADH + H+ (#40# immobilized
	HLAD shows about 95% reaction rate and free HLAD shows about 90%
	reaction rate with butanol compared to ethanol at pH 8.8 and 30°C
	<204>) |#111# 359% activity compared to cyclohexanone <197>| <197,204>
SP	#40,41,54# butyraldehyde + NADH = n-butanol + NAD+ (#41# activity with
	enzyme form ADH I, no activity with enzyme form ADH II <68>) {r}
	<42,68,99>
SP	#40,45# acetone + NADH = isopropanol + NAD+ {r} <31,66>
SP	#40,45# butan-2-one + NADH = butan-2-ol + NAD+ {r} <31,66>
SP	#40,45# pentan-3-ol + NAD+ = 3-pentanone + NADH {r} <31,66>
SP	#40,45# pentan-3-ol + NAD+ = 3-pentanone + NADH <31,66>
SP	#40,77# 4-methyl-1-pentanol + NAD+ = 4-methyl-1-pentanal + NADH {}
	<61,92>
SP	#40,77# 4-methyl-1-pentanol + NAD+ = 4-methyl-1-pentanal + NADH <61,92>
SP	#40,92# (R)-2-octanol + NAD+ = 2-octanone + NADH + H+ (#92# 2406% of
	the activity with 2-propanol <137>) {} <31,137>
SP	#40,92# (R)-2-octanol + NAD+ = 2-octanone + NADH + H+ (#92# 2406% of
	the activity with 2-propanol <137>) {r} <31,137>
SP	#40,92# (S)-2-octanol + NAD+ = 2-octanone + NADH + H+ (#92# 81% of the
	activity with 2-propanol <137>) {} <31,137>
SP	#40,92# (S)-2-octanol + NAD+ = 2-octanone + NADH + H+ (#92# 81% of the
	activity with 2-propanol <137>) {r} <31,137>
SP	#40,92,104# (R)-2-pentanol + NAD+ = 2-pentanone + NADH + H+ (#92# 75%
	of the activity with 2-propanol <137>) {} <31,137,207>
SP	#40,92,104# (R)-2-pentanol + NAD+ = 2-pentanone + NADH + H+ (#92# 75%
	of the activity with 2-propanol <137>) {r} <31,137,207>
SP	#40,92,104# (S)-2-pentanol + NAD+ = 2-pentanone + NADH + H+ (#92# 25%
	of the activity with 2-propanol <137>) {} <31,137,207>
SP	#40,92,104# (S)-2-pentanol + NAD+ = 2-pentanone + NADH + H+ (#92# 25%
	of the activity with 2-propanol <137>) {r} <31,137,207>
SP	#41# n-pentylaldehyde + NADH + H+ = n-pentanol + NAD+ {r} <68>
SP	#41# furfural + NADH = furfuryl alcohol + NADH (#41# activity with
	enzyme form ADH I, no activity with enzyme form ADH II <68>) {r} <68>
SP	#43# alcohol + NAD+ = aldehyde or ketone + NADH (#43# medium chain
	sec-alcohols or (omega-1)-ketones, no activity with primary alcohols or
	aldehydes <114>) {r} <114>
SP	#43# 4-chloroacetophenone + NADH = 1-(4-chlorophenyl)ethanol + NAD+ {r}
	<232>
SP	#43# capronaldehyde + NADH = 1-hexanol + NAD+ (#43# best substrate
	<232>) {r} <232>
SP	#43# phenylacetaldehyde + NADH = phenylethanol + NAD+ {r} <232>
SP	#43# valeraldehyde + NADH = 1-pentanol + NAD+ {r} <232>
SP	#45# 3-methylbutan-2-one + NADH = 3-methylbutan-2-ol + NAD+ <66>
SP	#45# cyclopetanone + NADH = cyclopentanol + NADH <66>
SP	#45# 3-methylcyclohexanol + NAD+ = 3-methylcyclohexanone + NADH {r} <66>
SP	#45# anisaldehyde + NADH = anisic alcohol + NADH <66,70>
SP	#45# 3-bromobenzyl alcohol + NAD+ = 3-bromobenzaldehyde + NADH + H+
	<153>
SP	#45# 3-bromobenzylalcohol + NAD+ = 3-bromobenzaldehyde + NADH + H+ <163>
SP	#45# 3-methoxybenzylalcohol + NAD+ = 3-methoxybenzaldehyde + NADH + H+
	<163>
SP	#45# 3-methylbutan-2-one + NADH + H+ = 3-methylbutan-2-ol + NAD+ <155>
SP	#45# 4-bromobenzyl alcohol + NAD+ = 4-bromobenzaldehyde + NADH + H+
	<153>
SP	#45# 4-bromobenzylalcohol + NAD+ = 4-bromobenzaldehyde + NADH + H+ <163>
SP	#45# 4-carboxybenzaldehyde + NADH + H+ = 4-carboxybenzyl alcohol + NAD+
	<153>
SP	#45# 4-carboxybenzaldehyde + NADH + H+ = 4-carboxybenzylalcohol + NAD+
	<163>
SP	#45# 4-methoxybenzylalcohol + NAD+ = 4-methoxybenzaldehyde + NADH + H+
	{r} <163>
SP	#45# 4-nitrobenzaldehyde + NADH + H+ = 4-nitrobenzylalcohol + NAD+ <163>
SP	#45# anisaldehyde + NADH + H+ = anisic alcohol + NAD+ <155>
SP	#45# benzyl aclohol + NAD+ = benzaldehyde + NADH + H+ <165>
SP	#45,122# 3-methylcyclohexanone + NADH = 3-methylcyclohexanol + NAD+
	(#122# about 10% of the activity compared to isatin <219>) {r} <66,219>
SP	#45,122# 3-methylcyclohexanone + NADH = 3-methylcyclohexanol + NAD+
	(#122# about 10% of the activity compared to isatin <219>) <66,219>
SP	#45,127# 4-nitrobenzaldehyde + NADH + H+ = 4-nitrobenzyl alcohol + NAD+
	<153,225>
SP	#45,127# 4-nitrobenzaldehyde + NADH + H+ = 4-nitrobenzyl alcohol + NAD+
	{r} <153,225>
SP	#45,56,100,109,110,111,126# 2-propanol + NAD+ = 2-propanone + NADH + H+
	(#100# activity is 3.1fold higher than with (S)-N-benzyl-3-pyrrolidinol
	<185>; #111# 6% activity compared to cyclohexanol <197>; #110# 73.5%
	activity compared to ethanol <213>) <147,153,163,185,197,210,213,222>
SP	#45,56,100,109,110,111,126# 2-propanol + NAD+ = 2-propanone + NADH + H+
	(#100# activity is 3.1fold higher than with (S)-N-benzyl-3-pyrrolidinol
	<185>; #111# 6% activity compared to cyclohexanol <197>; #110# 73.5%
	activity compared to ethanol <213>) {r}
	<147,153,163,185,197,210,213,222>
SP	#45,56,91,97,104,111,131,132# 1-propanol + NAD+ = propanal + NADH + H+
	(#97# about 75% of activity with ethanol, ADH1 <172>; #111# 153%
	activity compared to cyclohexanol <197>; #132# the enzyme shows a
	preference for short-chain alcohols ethanol and 1-propanol <237>)
	<144,147,153,154,163,172,197,207,237,239>
SP	#45,56,91,97,104,111,131,132# 1-propanol + NAD+ = propanal + NADH + H+
	(#97# about 75% of activity with ethanol, ADH1 <172>; #111# 153%
	activity compared to cyclohexanol <197>; #132# the enzyme shows a
	preference for short-chain alcohols ethanol and 1-propanol <237>) {r}
	<144,147,153,154,163,172,197,207,237,239>
SP	#45,60# butyraldehyde + NADH + H+ = n-butanol + NAD+ (#60# best
	substrate for isozyme ADH II <113>) <113,158>
SP	#45,60# butyraldehyde + NADH + H+ = n-butanol + NAD+ (#60# best
	substrate for isozyme ADH II <113>) {r} <113,158>
SP	#45,91,93# benzylalcohol + NAD+ = benzaldehyde + NADH + H+ (#91# weak
	activity <144>) {r} <144,162,163>
SP	#45,91,93# benzylalcohol + NAD+ = benzaldehyde + NADH + H+ (#91# weak
	activity <144>) <144,162,163>
SP	#46# 1-octanol + NAD+ = octanal + NADH (#46# 101% of the activity with
	2-phenylethanol <149>) <149>
SP	#46# 1-dodecanol + NAD+ = dodecanal + NADH (#46# 68% of the activity
	with 2-phenylethanol <149>) <149>
SP	#46# (R)-2-phenylpropanol + NAD+ = (R)-2-phenylpropanal + NADH + H+
	(#46# 63% of the activity with 2-phenylethanol <149>) <149>
SP	#46# (S)-2-phenylpropanol + NAD+ = (S)-2-phenylpropanal + NADH + H+
	(#46# 156% of the activity with 2-phenylethanol <149>) <149>
SP	#46# 2-phenylethanol + NAD+ = phenylacetaldehyde + NADH + H+ {r} <149>
SP	#46# 3-phenylpropanol + NAD+ = 3-phenylpropanal + NADH + H+ (#46# 135%
	of the activity with 2-phenylethanol <149>) <149>
SP	#46,57# 1-butanol + NAD+ = butanal + NADH (#46# 111% of the activity
	with 2-phenylethanol <149>) <147,149>
SP	#46,57,98# 2-propanol + NAD+ = 2-propanone + NADH (#46# 54% of the
	activity with 2-phenylethanol <149>) <147,149,173>
SP	#46,98# 1-phenylethanol + NAD+ = 1-phenylethanone + NADH (#46# 46% of
	the activity with 2-phenylethanol <149>) <149,173>
SP	#47# 1,2-propanediol + NAD+ = ? <223>
SP	#47# 1,3-propanediol + NAD+ = ? <223>
SP	#47,111# 2-mercaptoethanol + NAD+ = ? (#111# 11% activity compared to
	cyclohexanol <197>) <197,223>
SP	#47,126# 1-propanol + NAD+ = propanaldehyde + NADH + H+ {r} <222,223>
SP	#48# rac-3-methylcyclohexanone + NADH + H+ =
	(1S,3S)-3-methylcyclohexanol + NAD+ <166>
SP	#5# p-nitrobenzaldehyde + NADH = p-nitrobenzyl alcohol + NAD+ <48>
SP	#5# hexanol + NAD+ = hexaldehyde + NADH <119>
SP	#5# a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#5# ADH3 is
	involved in multiple cellular pathways, as diverse as formaldehyde
	detoxification, retinoid metabolism and NO homeostasis, ADH3 is
	considered to play only a minor role in hepatic alcohol metabolism
	because ethanol concentrations rarely exceed 50 mM <200>) <200>
SP	#5,10,40# allyl alcohol + NAD+ = acrolein + NADH |#5# product is toxic
	in mouse hepatocytes due to cell protein carbonylation following
	exposure to crotyl alcohol <117>| <117,120>
SP	#5,10,40# allyl alcohol + NAD+ = acrolein + NADH |#5# product is toxic
	in mouse hepatocytes due to cell protein carbonylation following
	exposure to crotyl alcohol <117>| {r} <117,120>
SP	#5,10,41,54# formaldehyde + NADH + H+ = methanol + NAD+ (#41# activity
	with ADH I, no activity with ADH II <68>; #5# reduced by isoenzyme A2,
	no activity with isoenzyme B2 and C2 <48>) <48,68,99,187,285>
SP	#5,10,41,54# formaldehyde + NADH + H+ = methanol + NAD+ (#41# activity
	with ADH I, no activity with ADH II <68>; #5# reduced by isoenzyme A2,
	no activity with isoenzyme B2 and C2 <48>) {r} <48,68,99,187,285>
SP	#5,31# (E)-hex-2-en-1-ol + NAD+ = (E)-hex-2-en-1-one + NADH (#31# 43.2%
	of the activity with ethanol <73>) <48,73>
SP	#5,40,87# crotyl alcohol + NAD+ = crotonaldehyde + NADH (#40# product
	is toxic in mouse hepatocytes due to cell protein carbonylation
	following exposure to crotyl alcohol <117>) |#5# product is toxic in
	mouse hepatocytes due to cell protein carbonylation following exposure
	to crotyl alcohol <117>| <117,118>
SP	#5,8# 7-cis-retinol + NAD+ = 7-cis-retinal + NADH <119>
SP	#5,8# octanol + NAD+ = octanal + NADH <110,115,200>
SP	#5,8,10,20,30,40,41,45,47,50,56,70,85,90,91,93,94,98,99,101,104,105,106
	107,108,109,110,111,118,124,125,126,131,132,135,136,137,138,154#
	ethanol + NAD+ = acetaldehyde + NADH + H+ (#47# best substrate <223>;
	#110# 100% activity <213>; #99# no activity with NADP+, in reverse
	reaction no activity with NADPH <171>; #30# the enzyme is highly
	specific for ethanol with NAD+ as the coenzyme <181>; #111# 88%
	activity compared to cyclohexanol <197>; #105# substrate for isozyme
	ADH1C, extremely poor substrate for isozyme ADH3 <214>; #105# substrate
	for isozyme ADH2 <214>; #108# substrate for isozyme ADH4 <214>; #132#
	the enzyme shows a preference for short-chain alcohols ethanol and
	1-propanol <237>; #154# 12% of the activity with butan-1-ol <271>)
	|#118# 83% of the activity with butan-2-ol <256>|
	<66,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181
	194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233
	237,239,246,252,256,271,279,284>
SP	#5,8,10,20,30,40,41,45,47,50,56,70,85,90,91,93,94,98,99,101,104,105,106
	107,108,109,110,111,118,124,125,126,131,132,135,136,137,138,154#
	ethanol + NAD+ = acetaldehyde + NADH + H+ (#47# best substrate <223>;
	#110# 100% activity <213>; #99# no activity with NADP+, in reverse
	reaction no activity with NADPH <171>; #30# the enzyme is highly
	specific for ethanol with NAD+ as the coenzyme <181>; #111# 88%
	activity compared to cyclohexanol <197>; #105# substrate for isozyme
	ADH1C, extremely poor substrate for isozyme ADH3 <214>; #105# substrate
	for isozyme ADH2 <214>; #108# substrate for isozyme ADH4 <214>; #132#
	the enzyme shows a preference for short-chain alcohols ethanol and
	1-propanol <237>; #154# 12% of the activity with butan-1-ol <271>)
	|#118# 83% of the activity with butan-2-ol <256>| {r}
	<66,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181
	194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233
	237,239,246,252,256,271,279,284>
SP	#5,8,10,20,30,40,41,45,47,50,56,70,85,90,91,93,94,98,99,101,104,105,106
	107,108,109,110,111,118,124,125,126,131,132,135,136,137,138,154#
	ethanol + NAD+ = acetaldehyde + NADH + H+ (#47# best substrate <223>;
	#110# 100% activity <213>; #99# no activity with NADP+, in reverse
	reaction no activity with NADPH <171>; #30# the enzyme is highly
	specific for ethanol with NAD+ as the coenzyme <181>; #111# 88%
	activity compared to cyclohexanol <197>; #105# substrate for isozyme
	ADH1C, extremely poor substrate for isozyme ADH3 <214>; #105# substrate
	for isozyme ADH2 <214>; #108# substrate for isozyme ADH4 <214>; #132#
	the enzyme shows a preference for short-chain alcohols ethanol and
	1-propanol <237>; #154# 12% of the activity with butan-1-ol <271>)
	|#118# 83% of the activity with butan-2-ol <256>| {}
	<66,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181
	194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233
	237,239,246,252,256,271,279,284>
SP	#5,8,35,40# all-trans-retinol + NAD+ = all-trans-retinal + NADH (#8#
	ADH4 might be involved in biosynthesis of retinoic acid <124>)
	<47,53,93,95,107,119,124,200>
SP	#5,8,35,40# all-trans-retinol + NAD+ = all-trans-retinal + NADH (#8#
	ADH4 might be involved in biosynthesis of retinoic acid <124>) {r}
	<47,53,93,95,107,119,124,200>
SP	#5,8,35,40,41,69,82# hexanol + NAD+ = n-hexanal + NADH (#41# activity
	with ADH I, no activity with ADH II <68>)
	<20,21,42,48,53,68,84,92,95,101>
SP	#5,8,35,40,41,69,82# hexanol + NAD+ = n-hexanal + NADH (#41# activity
	with ADH I, no activity with ADH II <68>) {}
	<20,21,42,48,53,68,84,92,95,101>
SP	#5,8,37,68# ethylene glycol + NAD+ = ? + NADH (#68# no activity <60>;
	#8# class III isoenzyme chi-ADH shows no activity <16>; #5# oxidized by
	isoenzyme A2, no activity with isoenzyme B2 and C2 <48>)
	<13,14,16,48,60,85>
SP	#5,8,37,68# ethylene glycol + NAD+ = ? + NADH (#68# no activity <60>;
	#8# class III isoenzyme chi-ADH shows no activity <16>; #5# oxidized by
	isoenzyme A2, no activity with isoenzyme B2 and C2 <48>) {}
	<13,14,16,48,60,85>
SP	#5,8,40# 9-cis-retinol + NAD+ = 9-cis-retinal + NADH <93,119>
SP	#5,8,40# 11-cis-retinol + NAD+ = 11-cis-retinal + NADH <93,119>
SP	#5,8,40# 13-cis-retinol + NAD+ = 13-cis-retinal + NADH (#5,8# no
	activity with isozyme ADH1 <119>) <93,119>
SP	#5,8,40,42,69,78# pentanol + NAD+ = pentanone + NADH (#5# oxidized by
	isoenzyme A2 and B2, no activity with isoenzyme C2 <48>)
	<14,16,18,20,24,25,48,53,84,92,96>
SP	#5,8,9,12,18,37,41,42,51,52,56,57,68,69,78,82,87,98,99,110# methanol +
	NAD+ = formaldehyde + NADH + H+ (#8,18,37,41,68,69# no activity
	<21,60,67,68,75,84,85>; #87# low activity <118>; #51# reaction is
	extremly weak <82>; #8# anodic enzyme form shows no activity <18>; #12#
	no activity at pH 7.5, slight activity at pH 10.8 <45>; #5# weak
	activity with isoenzyme A2, no activity with isoenzyme B2 and C2 <48>;
	#9# oxidized with ADH-3, no activity with ADH-1 and ADH-2 <49>; #8#
	class I isoenzymes <13>; #8# no activity with isoenzyme beta3,beta3
	<20>; #78# reaction is catalyzed by the pyrazole-sensitive enzyme, no
	activity with the pyrazole-insensitive enzyme <24>; #42# reaction is
	catalyzed by the cathodic pyrazole-sensitive enzyme, no activity by the
	cathodic pyrazole-insensitive enzyme and by the anodic
	pyrazole-insensitive enzyme <25>; #8# activity detected with class II
	isoenzyme pi-ADH <14>; #8# oxidized by isoenzyme beta1,beta1 <20>; #8#
	class III isoenzyme chi-ADH shows no activity <16>; #8# no activity
	with class III enzyme <11>; #110# 49.9% activity compared to ethanol
	<213>)
	<11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,67,68,75,82,84,85,101,118
	147,171,173,213>
SP	#5,8,9,12,18,37,41,42,51,52,56,57,68,69,78,82,87,98,99,110# methanol +
	NAD+ = formaldehyde + NADH + H+ (#8,18,37,41,68,69# no activity
	<21,60,67,68,75,84,85>; #87# low activity <118>; #51# reaction is
	extremly weak <82>; #8# anodic enzyme form shows no activity <18>; #12#
	no activity at pH 7.5, slight activity at pH 10.8 <45>; #5# weak
	activity with isoenzyme A2, no activity with isoenzyme B2 and C2 <48>;
	#9# oxidized with ADH-3, no activity with ADH-1 and ADH-2 <49>; #8#
	class I isoenzymes <13>; #8# no activity with isoenzyme beta3,beta3
	<20>; #78# reaction is catalyzed by the pyrazole-sensitive enzyme, no
	activity with the pyrazole-insensitive enzyme <24>; #42# reaction is
	catalyzed by the cathodic pyrazole-sensitive enzyme, no activity by the
	cathodic pyrazole-insensitive enzyme and by the anodic
	pyrazole-insensitive enzyme <25>; #8# activity detected with class II
	isoenzyme pi-ADH <14>; #8# oxidized by isoenzyme beta1,beta1 <20>; #8#
	class III isoenzyme chi-ADH shows no activity <16>; #8# no activity
	with class III enzyme <11>; #110# 49.9% activity compared to ethanol
	<213>) {r}
	<11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,67,68,75,82,84,85,101,118
	147,171,173,213>
SP	#5,8,9,12,18,37,41,42,51,52,56,57,68,69,78,82,87,98,99,110# methanol +
	NAD+ = formaldehyde + NADH + H+ (#8,18,37,41,68,69# no activity
	<21,60,67,68,75,84,85>; #87# low activity <118>; #51# reaction is
	extremly weak <82>; #8# anodic enzyme form shows no activity <18>; #12#
	no activity at pH 7.5, slight activity at pH 10.8 <45>; #5# weak
	activity with isoenzyme A2, no activity with isoenzyme B2 and C2 <48>;
	#9# oxidized with ADH-3, no activity with ADH-1 and ADH-2 <49>; #8#
	class I isoenzymes <13>; #8# no activity with isoenzyme beta3,beta3
	<20>; #78# reaction is catalyzed by the pyrazole-sensitive enzyme, no
	activity with the pyrazole-insensitive enzyme <24>; #42# reaction is
	catalyzed by the cathodic pyrazole-sensitive enzyme, no activity by the
	cathodic pyrazole-insensitive enzyme and by the anodic
	pyrazole-insensitive enzyme <25>; #8# activity detected with class II
	isoenzyme pi-ADH <14>; #8# oxidized by isoenzyme beta1,beta1 <20>; #8#
	class III isoenzyme chi-ADH shows no activity <16>; #8# no activity
	with class III enzyme <11>; #110# 49.9% activity compared to ethanol
	<213>) {ir}
	<11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,67,68,75,82,84,85,101,118
	147,171,173,213>
SP	#5,8,9,12,18,37,41,42,51,52,56,57,68,69,78,82,87,98,99,110# methanol +
	NAD+ = formaldehyde + NADH + H+ (#8,18,37,41,68,69# no activity
	<21,60,67,68,75,84,85>; #87# low activity <118>; #51# reaction is
	extremly weak <82>; #8# anodic enzyme form shows no activity <18>; #12#
	no activity at pH 7.5, slight activity at pH 10.8 <45>; #5# weak
	activity with isoenzyme A2, no activity with isoenzyme B2 and C2 <48>;
	#9# oxidized with ADH-3, no activity with ADH-1 and ADH-2 <49>; #8#
	class I isoenzymes <13>; #8# no activity with isoenzyme beta3,beta3
	<20>; #78# reaction is catalyzed by the pyrazole-sensitive enzyme, no
	activity with the pyrazole-insensitive enzyme <24>; #42# reaction is
	catalyzed by the cathodic pyrazole-sensitive enzyme, no activity by the
	cathodic pyrazole-insensitive enzyme and by the anodic
	pyrazole-insensitive enzyme <25>; #8# activity detected with class II
	isoenzyme pi-ADH <14>; #8# oxidized by isoenzyme beta1,beta1 <20>; #8#
	class III isoenzyme chi-ADH shows no activity <16>; #8# no activity
	with class III enzyme <11>; #110# 49.9% activity compared to ethanol
	<213>) {}
	<11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,67,68,75,82,84,85,101,118
	147,171,173,213>
SP	#5,8,9,18,35,40,45,57,68# benzyl alcohol + NAD+ = benzaldehyde + NADH
	(#18# no activity <75>; #5# oxidized by isoenzyme A2 and C2 no activity
	with isoenzyme B2 <48>; #9# oxidation with isoenzyme ADH-1 and ADH-3,
	no activity with isoenzyme ADH-2 <49>) {r}
	<13,14,16,42,47,48,49,60,66,70,75,96,110,147>
SP	#5,8,9,18,35,40,45,57,68# benzyl alcohol + NAD+ = benzaldehyde + NADH
	(#18# no activity <75>; #5# oxidized by isoenzyme A2 and C2 no activity
	with isoenzyme B2 <48>; #9# oxidation with isoenzyme ADH-1 and ADH-3,
	no activity with isoenzyme ADH-2 <49>)
	<13,14,16,42,47,48,49,60,66,70,75,96,110,147>
SP	#5,8,9,18,35,40,45,57,68# benzyl alcohol + NAD+ = benzaldehyde + NADH
	(#18# no activity <75>; #5# oxidized by isoenzyme A2 and C2 no activity
	with isoenzyme B2 <48>; #9# oxidation with isoenzyme ADH-1 and ADH-3,
	no activity with isoenzyme ADH-2 <49>) {}
	<13,14,16,42,47,48,49,60,66,70,75,96,110,147>
SP	#5,8,9,18,35,42,66,68,77,80,82# cyclohexanol + NAD+ = cyclohexanone +
	NADH (#18# no activity <75>; #5# oxidized by isoenzyme A2, no activity
	with isoenzymes B2 and C2 <48>; #42# reaction is catalyzed by the
	cathodic pyrazole-sensitive enzyme, no activity with the cathodic
	pyrazole-insensitive enzyme and by the anodic pyrazole-insensitive
	enzyme <25>) <13,14,25,47,48,49,60,61,75,77,78,95,101>
SP	#5,8,9,18,35,42,66,68,77,80,82# cyclohexanol + NAD+ = cyclohexanone +
	NADH (#18# no activity <75>; #5# oxidized by isoenzyme A2, no activity
	with isoenzymes B2 and C2 <48>; #42# reaction is catalyzed by the
	cathodic pyrazole-sensitive enzyme, no activity with the cathodic
	pyrazole-insensitive enzyme and by the anodic pyrazole-insensitive
	enzyme <25>) {} <13,14,25,47,48,49,60,61,75,77,78,95,101>
SP	#5,8,9,18,37,41,42,68,69,82# octan-1-ol + NAD+ = n-octanal + NADH (#69#
	weak activity <84>; #41# activity with ADH I, no activity with ADH II
	<68>) <11,13,14,21,25,48,49,60,68,75,84,85,101>
SP	#5,84,121# benzaldehyde + NADH = benzyl alcohol + NAD+ (#5# reduced by
	isoenzyme A2 and C2, no activity with isoenzyme B2 <48>) <48,217,226>
SP	#5,84,121# benzaldehyde + NADH = benzyl alcohol + NAD+ (#5# reduced by
	isoenzyme A2 and C2, no activity with isoenzyme B2 <48>) {r}
	<48,217,226>
SP	#52# hexadecanol + NAD+ = hexadecanal + NADH (#52# very low activity
	<59>) <59>
SP	#53# 2-methylbutyraldehyde + NADH + H+ = 2-methylbutanol + NAD+ (#53#
	1.4% of the activity with acetaldehyde <151>) <151>
SP	#53# 2-methylpropionaldehyde + NADH + H+ = 2-methylpropanal + NAD+
	(#53# 3.3% of the activity with acetaldehyde <151>) <151>
SP	#53# 3-methylbutyraldehyde + NADH + H+ = 3-methylbutanol + NAD+ (#53#
	2.9% of the activity with acetaldehyde <151>) <151>
SP	#53# butyraldehyde + NADH + H+ = butanol + NAD+ (#53# 56% of the
	activity with acetaldehyde <151>) <151>
SP	#53# butyraldehyde + NADPH + H+ = butanol + NADP+ (#53# 22% of the
	activity with NADH <151>) <151>
SP	#53# hexanal + NADH + H+ = 1-hexanone + NAD+ (#53# 49% of the activity
	with acetaldehyde <151>) <151>
SP	#53# hexanal + NADPH + H+ = 1-hexanone + NADP+ (#53# 24% of the
	activity with NADH <151>) <151>
SP	#53,143,146# acetaldehyde + NADPH + H+ = ethanol + NADP+ (#53# 16% of
	the activity with NADH <151>; #143# NADPH is not a cofactor for
	wild-type, but for mutant P704L/H734R <265>) {r} <151,259,265>
SP	#53,143,146# acetaldehyde + NADPH + H+ = ethanol + NADP+ (#53# 16% of
	the activity with NADH <151>; #143# NADPH is not a cofactor for
	wild-type, but for mutant P704L/H734R <265>) <151,259,265>
SP	#54# 1,3-propanediol + NAD+ = ? + NADH (#54# 7% of the activity with
	ethanol <99>) <99>
SP	#54,67# propan-1,2-diol + NAD+ = ? + NADH <69,99>
SP	#56# 1,2-propanediol + NAD+ = hydroxyacetone + NADH + H+ <147>
SP	#56# glycerol + NAD+ = dihydroxyacetone + NADH + H+ <147>
SP	#57# 1,2-propanediol + NAD+ = hydroxyacetone + NADH <147>
SP	#57# 1-propanol + NAD+ = propanal + NADH <147>
SP	#57,89# glycerol + NAD+ = dihydroxyacetone + NADH <105,147>
SP	#6# 1-(4'-chlorophenyl)ethanol + NAD+ = 1-(4'-chlorophenyl)ethanone +
	NADH + H+ (#6# 26% of the activity with (S)-(-)-1-phenylethanol <169>)
	<169>
SP	#6# 1-phenyl-1-propanol + NAD+ = 1-phenyl-1-propanone + NADH + H+ (#6#
	59% of the activity with (S)-(-)-1-phenylethanol <169>) <169>
SP	#6# 2,2,2-trifluoroacetophenone + NADH + H+ =
	(R)-alpha-(trifluoromethyl)benzyl alcohol + NAD+ (#6# 93% enantiomeric
	excess <169>) |#6# 93% enantiomeric excess <169>| {r} <169>
SP	#6# 2,2,2-trifluoroacetophenone + NADH + H+ =
	(R)-alpha-(trifluoromethyl)benzyl alcohol + NAD+ (#6# 93% enantiomeric
	excess <169>) |#6# 93% enantiomeric excess <169>| <169>
SP	#6# 2-methoxybenzaldehyde + NADH + H+ = 2-methoxybenzylalcohol + NAD+
	(#6# 13% of the activity with 2,2,2-trifluoroacetophenone <169>) <169>
SP	#6# 2-methoxybenzyl alcohol + NAD+ = 2-methoxybenzaldehyde + NADH + H+
	(#6# 25% of the activity with (S)-(-)-1-phenylethanol <169>) <169>
SP	#6# 3-methoxybenzaldehyde + NADH + H+ = 3-methoxybenzylalcohol + NAD+
	(#6# 14% of the activity with 2,2,2-trifluoroacetophenone <169>) <169>
SP	#6# 4'-chlorobutyrophenone + NADH + H+ = 1-(4-chlorophenyl)butan-1-ol +
	NAD+ (#6# 10% of the activity with 2,2,2-trifluoroacetophenone <169>)
	<169>
SP	#6# 4-methoxybenzaldehyde + NADH + H+ = 4-methoxybenzylalcohol + NAD+
	(#6# 13% of the activity with 2,2,2-trifluoroacetophenone <169>) <169>
SP	#6# acetophenone + NADH + H+ = (S)-(-)-1-phenylethanol + NAD+ (#6# more
	than 99% enantiomeric excess <169>) {r} <169>
SP	#6# acetophenone + NADH + H+ = (S)-1-phenylethanol + NAD+ |#6# 99%
	enantiomeric excess <169>| {r} <169>
SP	#6# alpha-tetralone + NADH + H+ = (S)-alpha-tetralol + NAD+ (#6# more
	than 99% enantiomeric excess <169>) |#6# 99% enantiomeric excess <169>|
	{r} <169>
SP	#6# alpha-tetralone + NADH + H+ = (S)-alpha-tetralol + NAD+ (#6# more
	than 99% enantiomeric excess <169>) |#6# 99% enantiomeric excess <169>|
	<169>
SP	#6# ethyl benzoylformate + NADH + H+ = ethyl (R)-(-)-mandelate + NAD+
	(#6# 95% enantiomeric excess <169>) <169>
SP	#6# methyl benzoylformate + NADH + H+ = methyl (R)-(-)-mandelate + NAD+
	(#6# 92% enantiomeric excess <169>) <169>
SP	#6# methylbenzoylformate + NADH + H+ = ? (#6# 13% of the activity with
	2,2,2-trifluoroacetophenone <169>) <169>
SP	#6# trans-cinnamyl alcohol + NAD+ = (2E)-3-phenylprop-2-enal + NADH +
	H+ (#6# activity is 3.9fold higher than with (S)-(-)-1-phenylethanol
	<169>) <169>
SP	#6# (S)-(+)-1-indanol + NAD+ = indanone + NADH + H+ <169>
SP	#6# (S)-1-phenylethanol + NAD+ = 1-phenylethanone + NADH + H+ {r} <169>
SP	#6# 1-(4'-fluorophenyl)ethanol + NAD+ = 1-(4'-fluorophenyl)ethanone +
	NADH + H+ (#6# 45% of the activity with (S)-1-phenylethanol <169>) {r}
	<169>
SP	#6# 1-indanone + NADH + H+ = 1-indanol + NAD+ {r} <169>
SP	#6# 1-phenyl-1,2-propandione + NADH + H+ =
	1-phenyl-2-hydroxy-1-propanone + NAD+ (#6# 146% of the activity with
	2,2,2-trifluoroacetophenone <169>) {r} <169>
SP	#6# 1-phenyl-1-propanol + NAD+ = 1-phenylpropanal + NADH + H+ (#6# 59%
	of the activity with (S)-1-phenylethanol <169>) {r} <169>
SP	#6# 3-methoxybenzaldehyde + NADH + H+ = 3-methoxybenzyl alcohol + NAD+
	{r} <169>
SP	#6# alpha-ethyl benzoylformate + NADH + H+ = ethyl (R)-(-)-mandelate +
	NAD+ |#6# 95% enantiomeric excess <169>| {r} <169>
SP	#6# alpha-methyl benzoylformate + NADH + H+ = methyl (R)-mandelate +
	NAD+ |#6# 92% enantiomeric excess <169>| {r} <169>
SP	#6# alpha-tetralone + NADH + H+ = alpha-tetralol + NAD+ {r} <169>
SP	#6# ethyl oxo(phenyl)acetate + NADH + H+ = ethyl hydroxy(phenyl)acetate
	+ NAD+ (#6# 100% of the activity with 2,2,2-trifluoroacetophenone
	<169>) {r} <169>
SP	#6# methyl oxo(phenyl)acetate + NADH + H+ = methyl
	hydroxy(phenyl)acetate + NAD+ (#6# 57% of the activity with
	2,2,2-trifluoroacetophenone <169>) {r} <169>
SP	#6,10,91,92,97,112,131# 2-propanol + NAD+ = acetone + NADH + H+ (#97#
	about 50% of activity with ethanol, ADH1 <172>)
	<137,144,169,172,202,239>
SP	#6,10,91,92,97,112,131# 2-propanol + NAD+ = acetone + NADH + H+ (#97#
	about 50% of activity with ethanol, ADH1 <172>) {r}
	<137,144,169,172,202,239>
SP	#6,10,91,92,97,112,131# 2-propanol + NAD+ = acetone + NADH + H+ (#97#
	about 50% of activity with ethanol, ADH1 <172>) {ir}
	<137,144,169,172,202,239>
SP	#6,111,123# 1-indanol + NAD+ = 1-indanone + NADH + H+ (#123# 26% of the
	activity compared to isoborneol <218>) |#111# 1% activity compared to
	cyclohexanone <197>| <169,197,218>
SP	#6,111,123# 1-indanol + NAD+ = 1-indanone + NADH + H+ (#123# 26% of the
	activity compared to isoborneol <218>) |#111# 1% activity compared to
	cyclohexanone <197>| {r} <169,197,218>
SP	#6,111,149# 1-phenyl-2-propanol + NAD+ = 1-phenyl-2-propanone + NADH +
	H+ (#6# 16% of the activity with (S)-(-)-1-phenylethanol <169>; #111#
	3% activity compared to cyclohexanol <197>; #149# 39% of the activity
	with 1-phenylethanol <243>) <169,197,243>
SP	#6,111,149# 1-phenyl-2-propanol + NAD+ = 1-phenyl-2-propanone + NADH +
	H+ (#6# 16% of the activity with (S)-(-)-1-phenylethanol <169>; #111#
	3% activity compared to cyclohexanol <197>; #149# 39% of the activity
	with 1-phenylethanol <243>) {r} <169,197,243>
SP	#6,123# 1-phenyl-1,2-propanedione + NADH + H+ = ? (#6# activity is
	1.46fold higher than with 2,2,2-trifluoroacetophenone <169>; #123#
	1-phenyl-1,2-propanedione and ethyl 3-methyl-2-oxobutyrate are the best
	substrate in the reduction reaction <218>) <169,218>
SP	#6,123# 2,2-dichloroacetophenone + NADH + H+ =
	2,2-dichloro-1-phenylethanol + NAD+ (#6# 32% of the activity with
	2,2,2-trifluoroacetophenone <169>; #123# 30% of the activity compared
	to 1-phenyl-1,2-propanedione <218>) <169,218>
SP	#6,123# (S)-alpha-tetralol + NAD+ = alpha-tetralone + NADH + H+ (#6#
	2700% of the activity with (S)-1-phenylethanol <169>) {r} <169,219>
SP	#6,123# 2,2,2-trifluoroacetophenone + NADH + H+ =
	2,2,2-trifluoro-1-phenylethanol + NAD+ (#123# 35% of the activity
	compared to 1-phenyl-1,2-propanedione <218>) {r} <169,218>
SP	#6,123# 2,2,2-trifluoroacetophenone + NADH + H+ =
	2,2,2-trifluoro-1-phenylethanol + NAD+ (#123# 35% of the activity
	compared to 1-phenyl-1,2-propanedione <218>) <169,218>
SP	#6,123# (S)-1-indanol + NAD+ = 1-indanone + NADH + H+ (#6# 3900% of the
	activity with (S)-1-phenylethanol <169>) {r} <169,219>
SP	#6,149# 1-(4-fluorophenyl)ethanol + NAD+ = 1-(4-fluorophenyl)ethanone +
	NADH + H+ (#6# 45% of the activity with (S)-(-)-1-phenylethanol <169>;
	#149# 119% of the activity with 1-phenylethanol <243>) <169,243>
SP	#6,25,45,53,95,100,118,127# benzaldehyde + NADH + H+ = benzyl alcohol +
	NAD+ (#53# 1.2% of the activity with acetaldehyde <151>; #95# 3%
	activity compared to benzyl alcohol <156>; #6# 14% of the activity with
	2,2,2-trifluoroacetophenone <169>; #25# 21% of activity with
	N-benzyl-3-pyrrolidinone <188>; #100# 74% of the activity with
	N-benzyl-3-pyrrolidinone <185>) |#118# 93% of the activity with
	butan-2-ol <256>| <151,156,158,169,185,188,225,256>
SP	#6,25,45,53,95,100,118,127# benzaldehyde + NADH + H+ = benzyl alcohol +
	NAD+ (#53# 1.2% of the activity with acetaldehyde <151>; #95# 3%
	activity compared to benzyl alcohol <156>; #6# 14% of the activity with
	2,2,2-trifluoroacetophenone <169>; #25# 21% of activity with
	N-benzyl-3-pyrrolidinone <188>; #100# 74% of the activity with
	N-benzyl-3-pyrrolidinone <185>) |#118# 93% of the activity with
	butan-2-ol <256>| {r} <151,156,158,169,185,188,225,256>
SP	#6,45# 3-methoxybenzyl alcohol + NAD+ = 3-methoxybenzaldehyde + NADH +
	H+ (#6# 13% of the activity with (S)-(-)-1-phenylethanol <169>)
	<153,169>
SP	#6,45,104,111,131,142,149# cyclohexanol + NAD+ = cyclohexanone + NADH +
	H+ (#111# 100% activity <197>; #6# 13% of the activity with
	(S)-(-)-1-phenylethanol <169>; #142# 12% of the activity with
	2,3-butanediol <138>; #149# 52% of the activity with 1-phenylethanol
	<243>) |#111# 100% activity <197>| <138,153,154,163,169,197,207,239,243>
SP	#6,45,104,111,131,142,149# cyclohexanol + NAD+ = cyclohexanone + NADH +
	H+ (#111# 100% activity <197>; #6# 13% of the activity with
	(S)-(-)-1-phenylethanol <169>; #142# 12% of the activity with
	2,3-butanediol <138>; #149# 52% of the activity with 1-phenylethanol
	<243>) |#111# 100% activity <197>| {r}
	<138,153,154,163,169,197,207,239,243>
SP	#6,45,104,131# 4-methoxybenzyl alcohol + NAD+ = 4-methoxybenzaldehyde +
	NADH + H+ (#6# 99% of the activity with (S)-(-)-1-phenylethanol <169>;
	#6# 99% of the activity with (S)-1-phenylethanol <169>) {r}
	<153,154,169,207,239>
SP	#6,45,104,131# 4-methoxybenzyl alcohol + NAD+ = 4-methoxybenzaldehyde +
	NADH + H+ (#6# 99% of the activity with (S)-(-)-1-phenylethanol <169>;
	#6# 99% of the activity with (S)-1-phenylethanol <169>)
	<153,154,169,207,239>
SP	#6,8,10,13,25,35,40,41,45,47,50,51,52,53,59,60,70,77,84,87,89,91,92,95
	97,100,105,108,109,111,113,118,122,123,126,127,131,132,141,142,149,150
	152,154,159# more = ? (#13# broad substrate specificity <126>; #10#
	constitutive enzyme <94>; #41# key enzyme in ethanol production <68>;
	#51# one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
	<82>; #52# enzyme may be involved in the metabolism of dietary wax
	esters in salmonid fish <59>; #77# the enzyme oxidizes alcohols to
	aldehydes or ketones both for detoxification and metabolic purposes
	<38>; #35# involvement in the development of male hamster reproductive
	system <47>; #87# enzyme shows high substrate specificity towards
	primary aliphatic alcohols, no activity with 2-butanol, tert-butanol,
	isoamyl alcohol, isobutyl alcohol, 1,6-hexadiol, and mono-, di-, and
	triethanolamine <118>; #89# no activity with methanol, 2-propanol, and
	isoamyl alcohol <105>; #10# substrate specificity and
	stereospecificity, substrate binding pocket structure of the 3
	isozymes, involving Met294, Trp57, and Trp93 <120>; #60# substrate
	specificity of the 2 isozmyes with various substrates, overview,
	isozymes are highly specific for the (R)-stereoisomers and
	enantioselctive for the R(-)isomers <113>; #45# the enzyme undergoes a
	substantial conformational change in the apo-holo transition,
	accompanied by loop movements at the domain interface <108>; #59#
	alcohol dehydrogenase activity may not limit alcohol supply for ester
	production during ripening <146>; #53# Cm-ADH2 cannot reduce branched
	aldehydes <151>; #10# effects of pressure on deuterium isotope effects
	of yeast alcohol dehydrogenase using alternative substrates <139>; #91#
	no activity with methanol <144>; #92# the enzyme does not act on
	short-chain normal alkyl alcohols, including methanol and ethanol
	<137>; #95# no activity towards methanol, ethanol, 1-propanol,
	triethylene glycol, polyethylene glycol 400, polyethylene glycol 1000,
	D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, propionaldehyde,
	butyraldehyde, and valeraldehyde <156>; #97# ADH1 preferrs primary
	alcohols containing C3-C8 carbons to secondary alcohols such as
	2-propanol and 2-butanol. ADH1 possesses specific carboxylate
	ester-forming activity <172>; #100# no activity detected with:
	N-benzyl-2-pyrrolidinone, 2-pyrrolidinone, 3-hexanone,
	4-hydroxy-2-butanone, (R)-N-benzyl-3-pyrrolidinol, ethanol,
	1,3-propanediol, 1-butanol, 1,4-butanediol, 1,2,3-butanetriol,
	1,2,4-butanetriol, acetol, 2-phenyl-1-propanol, 3-phenyl-1-propanol,
	benzyl alcohol and glycerol. No activity with NADP+ or NADPH <185>; #6#
	preference for reduction of aromatic ketones and alpha-keto esters, and
	poor activity on aromatic alcohols and aldehydes <169>; #25# when NADH
	is replaced with NADPH, the reaction rate is reduced by 0.6% <188>;
	#40# activity is severely reduced towards aliphatic alcohols of more
	than 8 carbon atoms for the free enzyme, but not so with immobilized
	HLAD, exhibiting an activity towards C22 and C24 aliphatic alcohols
	higher than 50% of the highest value, obtained with C8 <204>; #8#
	differences in the activities of total ADH and class I ADH isoenzyme
	between cancer liver tissues and healthy hepatocytes may be a factor in
	ethanol metabolism disorders, which can intensify carcinogenesis <180>;
	#111# TADH is a NAD(H)-dependent enzyme and shows a very broad
	substrate spectrum producing exclusively the (S)-enantiomer in high
	enantiomeric excess (more than 99%) during asymmetric reduction of
	ketones <197>; #105# 1-octanal is no substrate for isozyme ADH1C <214>;
	#105# 1-octanal is no substrate for isozyme ADH2 <214>; #108# 1-octanal
	is no substrate for isozyme ADH4 <214>; #111# ADH exhibits a clear
	preference for primary alcohols and corresponding aldehydes for
	aliphatic substrates, in the oxidative direction activity steeply
	increases with chain length until 1-propanol and then decreases
	slightly again with growing chain length, alpha,beta-unsaturated
	ketones like 3-penten-2-one and cyclohexenone are not converted by ADH,
	almost no conversion of methanol (0.2%) and (+)-carvone (0.4%) is
	detected <197>; #109# no activity towards methanol <210>; #113#
	substrates are a broad range of alkyl alcohols from ethanol to
	1-triacontanol <215>; #122# the physiological direction of the
	catalytic reaction is reduction rather than oxidation <219>; #123# the
	enzyme displays a preference for the reduction of alicyclic, bicyclic
	and aromatic ketones and alpha-ketoesters, but is poorly active on
	aliphatic, cyclic and aromatic alcohols, showing no activity on
	aldehydes <218>; #122# the enzyme shows no activity on aliphatic linear
	and branched alcohols, except for a poor activity on 2-propyn-1-ol,
	3-methyl-1-butanol and 2-pentanol; however, it shows a discrete
	activity on aliphatic cyclic and bicyclic alcohols. Benzyl alcohol and
	4-bromobenzyl alcohol are not found to be substrates. The S and R
	enantiomers of a-(trifluoromethyl)benzyl alcohol and methyl and ethyl
	mandelates show no apparent activity with SaADH. The enzyme shows poor
	activity on (+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol and the
	two enantiomers of 1-(2-naphthyl)ethanol. The enzyme is not active on
	aliphatic and aromatic aldehydes, and on aliphatic linear, branched and
	cyclic ketones except for 3-methylcyclohexanone. Catalytic inactivity
	is observed with acetophenone and (S)-a-(trifluoromethyl)benzyl <219>;
	#126# methanol, formaldehyde, and acetone are no substrates for HpADH3
	<222>; #47# no activity with methanol, 1-butanol, glycerol or
	2-propanol <223>; #127# substrate specificity and enantiospecificity,
	overview. The (R)-specific alcohol dehydrogenase requires NADH and
	reduces various kinds of carbonyl compounds, including ketones and
	aldehydes. AFPDH reduces acetylpyridine derivatives, beta-keto esters,
	and some ketones compounds with high enantiospecificity, overview. No
	activity with 2-chlorobenzaldehyde and 2-tetralone, poor activity with
	1-tetralone, pyruvate, 2-oxobutyrate, oxalacetate, cyclopentanone,
	cyclohexanone, cycloheptanone, and dipropylketone. No activity with
	1,2-propanediol, 3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol,
	glycerol, 1-pentanol, poor activity with 1-butanol, 1-propanol,
	ethanol, and methanol <225>; #84# the enzyme exhibits broad substrate
	specificity towards aliphatic ketones, cycloalkanones, aromatic
	ketones, and ketoesters <226>; #131# the enzyme shows broad substrate
	specificity and prefers aliphatic alcohols and ketones. There are no
	large differences in the reactivities between primary and secondary
	alcohols. The enzyme produces (S)-alcohols from the corresponding
	ketones. The values of the enantiomeric excess increase with the
	increase of chain length except for the reduction of 2-hexanone. The
	highest enantioselectivity is shown with the reduction of 2-nonanone
	<239>; #132# the NAD+-dependent HvADH1 shows a preference for
	short-chain alcohols, no activity with methanol <237>; #142# broad
	substrate specificity with a preference for the reduction of ketones
	and the oxidation of secondary alcohols <138>; #123# enzyme displays a
	preference for the reduction of alicyclic, bicyclic and aromatic
	ketones and alpha-keto esters, but is poorly active on aliphatic,
	cyclic and aromatic alcohols, and shows no activity on aldehydes <219>;
	#149# enzyme reduces aldehydes to (R)-alcohols with more than 99.8%
	enantiomeric excess <243>; #150# enzyme selectively reduces the C=O
	bond of allylic aldehydes/ketones to the corresponding
	alpha,beta-unsaturated alcohols and also has the capacity of
	stereoselectively reducing aromatic ketones to (S)-enantioselective
	alcohols. The enzyme preferentially catalyzes oxidation of
	allylic/benzyl aldehydes <244>; #70# ethanol dehydrogenase activity of
	Thermoanaerobium brockii is both NAD and NADP linked, reversible, and
	not inhibited by low levels of reaction products <103>; #118,141#
	mutation at the substrate-binding site, or at a dimer interface, alters
	kinetic properties and protein oligomeric structure, active site
	flexibility is correlated with subunit interactions 20 A away <260>;
	#6# the enzyme transfers the pro-S hydrogen of [4R-(2)H]NADH and
	exhibits Prelog specificity <269>; #40# acycloNAD+ i.e. NAD+-analogue,
	where the nicotinamide ribosyl moiety has been replaced by the
	nicotinamide (2-hydroxyethoxy)methyl moiety. There is no detectable
	reduction of acycloNAD+ by secondary alcohols although these alcohols
	serve as competitive inhibitors. AcycloNAD+ converts horse liver ADH
	from a broad spectrum alcohol dehydrogenase, capable of utilizing
	either primary or secondary alcohols, into an exclusively primary
	alcohol dehydrogenase <275>; #50# bifunctional enzyme consisting of an
	N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol
	dehydrogenase (ADH). The specificity constant (kcat/Km) is 47fold
	higher for acetaldehyde reductase than that for ethanol dehydrogenase
	<279>; #152# enzyme is an alcohol dehydrogenase with additional
	activity for all-trans-retinol, reaction of EC 1.1.1.184 <272>; #154#
	enzyme shows activity as a reductase specific for (S)-acetoin, EC
	1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent
	alcohol dehydrogenase (EC 1.1.1.1) activities <271>; #159# the enzyme
	additionally catalyzes selective reduction of 3-quinuclidinone to
	(R)-3-quinuclidinol, with 84% ee and 62% conversion after 22 h <274>)
	{}
	<38,47,59,68,82,94,103,105,108,113,118,120,126,137,138,139,144,146,151
	156,169,172,180,185,188,197,204,210,211,214,215,218,219,222,223,225,226
	237,239,243,244,260,269,271,272,274,275,279>
SP	#6,8,10,13,25,35,40,41,45,47,50,51,52,53,59,60,70,77,84,87,89,91,92,95
	97,100,105,108,109,111,113,118,122,123,126,127,131,132,141,142,149,150
	152,154,159# more = ? (#13# broad substrate specificity <126>; #10#
	constitutive enzyme <94>; #41# key enzyme in ethanol production <68>;
	#51# one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
	<82>; #52# enzyme may be involved in the metabolism of dietary wax
	esters in salmonid fish <59>; #77# the enzyme oxidizes alcohols to
	aldehydes or ketones both for detoxification and metabolic purposes
	<38>; #35# involvement in the development of male hamster reproductive
	system <47>; #87# enzyme shows high substrate specificity towards
	primary aliphatic alcohols, no activity with 2-butanol, tert-butanol,
	isoamyl alcohol, isobutyl alcohol, 1,6-hexadiol, and mono-, di-, and
	triethanolamine <118>; #89# no activity with methanol, 2-propanol, and
	isoamyl alcohol <105>; #10# substrate specificity and
	stereospecificity, substrate binding pocket structure of the 3
	isozymes, involving Met294, Trp57, and Trp93 <120>; #60# substrate
	specificity of the 2 isozmyes with various substrates, overview,
	isozymes are highly specific for the (R)-stereoisomers and
	enantioselctive for the R(-)isomers <113>; #45# the enzyme undergoes a
	substantial conformational change in the apo-holo transition,
	accompanied by loop movements at the domain interface <108>; #59#
	alcohol dehydrogenase activity may not limit alcohol supply for ester
	production during ripening <146>; #53# Cm-ADH2 cannot reduce branched
	aldehydes <151>; #10# effects of pressure on deuterium isotope effects
	of yeast alcohol dehydrogenase using alternative substrates <139>; #91#
	no activity with methanol <144>; #92# the enzyme does not act on
	short-chain normal alkyl alcohols, including methanol and ethanol
	<137>; #95# no activity towards methanol, ethanol, 1-propanol,
	triethylene glycol, polyethylene glycol 400, polyethylene glycol 1000,
	D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, propionaldehyde,
	butyraldehyde, and valeraldehyde <156>; #97# ADH1 preferrs primary
	alcohols containing C3-C8 carbons to secondary alcohols such as
	2-propanol and 2-butanol. ADH1 possesses specific carboxylate
	ester-forming activity <172>; #100# no activity detected with:
	N-benzyl-2-pyrrolidinone, 2-pyrrolidinone, 3-hexanone,
	4-hydroxy-2-butanone, (R)-N-benzyl-3-pyrrolidinol, ethanol,
	1,3-propanediol, 1-butanol, 1,4-butanediol, 1,2,3-butanetriol,
	1,2,4-butanetriol, acetol, 2-phenyl-1-propanol, 3-phenyl-1-propanol,
	benzyl alcohol and glycerol. No activity with NADP+ or NADPH <185>; #6#
	preference for reduction of aromatic ketones and alpha-keto esters, and
	poor activity on aromatic alcohols and aldehydes <169>; #25# when NADH
	is replaced with NADPH, the reaction rate is reduced by 0.6% <188>;
	#40# activity is severely reduced towards aliphatic alcohols of more
	than 8 carbon atoms for the free enzyme, but not so with immobilized
	HLAD, exhibiting an activity towards C22 and C24 aliphatic alcohols
	higher than 50% of the highest value, obtained with C8 <204>; #8#
	differences in the activities of total ADH and class I ADH isoenzyme
	between cancer liver tissues and healthy hepatocytes may be a factor in
	ethanol metabolism disorders, which can intensify carcinogenesis <180>;
	#111# TADH is a NAD(H)-dependent enzyme and shows a very broad
	substrate spectrum producing exclusively the (S)-enantiomer in high
	enantiomeric excess (more than 99%) during asymmetric reduction of
	ketones <197>; #105# 1-octanal is no substrate for isozyme ADH1C <214>;
	#105# 1-octanal is no substrate for isozyme ADH2 <214>; #108# 1-octanal
	is no substrate for isozyme ADH4 <214>; #111# ADH exhibits a clear
	preference for primary alcohols and corresponding aldehydes for
	aliphatic substrates, in the oxidative direction activity steeply
	increases with chain length until 1-propanol and then decreases
	slightly again with growing chain length, alpha,beta-unsaturated
	ketones like 3-penten-2-one and cyclohexenone are not converted by ADH,
	almost no conversion of methanol (0.2%) and (+)-carvone (0.4%) is
	detected <197>; #109# no activity towards methanol <210>; #113#
	substrates are a broad range of alkyl alcohols from ethanol to
	1-triacontanol <215>; #122# the physiological direction of the
	catalytic reaction is reduction rather than oxidation <219>; #123# the
	enzyme displays a preference for the reduction of alicyclic, bicyclic
	and aromatic ketones and alpha-ketoesters, but is poorly active on
	aliphatic, cyclic and aromatic alcohols, showing no activity on
	aldehydes <218>; #122# the enzyme shows no activity on aliphatic linear
	and branched alcohols, except for a poor activity on 2-propyn-1-ol,
	3-methyl-1-butanol and 2-pentanol; however, it shows a discrete
	activity on aliphatic cyclic and bicyclic alcohols. Benzyl alcohol and
	4-bromobenzyl alcohol are not found to be substrates. The S and R
	enantiomers of a-(trifluoromethyl)benzyl alcohol and methyl and ethyl
	mandelates show no apparent activity with SaADH. The enzyme shows poor
	activity on (+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol and the
	two enantiomers of 1-(2-naphthyl)ethanol. The enzyme is not active on
	aliphatic and aromatic aldehydes, and on aliphatic linear, branched and
	cyclic ketones except for 3-methylcyclohexanone. Catalytic inactivity
	is observed with acetophenone and (S)-a-(trifluoromethyl)benzyl <219>;
	#126# methanol, formaldehyde, and acetone are no substrates for HpADH3
	<222>; #47# no activity with methanol, 1-butanol, glycerol or
	2-propanol <223>; #127# substrate specificity and enantiospecificity,
	overview. The (R)-specific alcohol dehydrogenase requires NADH and
	reduces various kinds of carbonyl compounds, including ketones and
	aldehydes. AFPDH reduces acetylpyridine derivatives, beta-keto esters,
	and some ketones compounds with high enantiospecificity, overview. No
	activity with 2-chlorobenzaldehyde and 2-tetralone, poor activity with
	1-tetralone, pyruvate, 2-oxobutyrate, oxalacetate, cyclopentanone,
	cyclohexanone, cycloheptanone, and dipropylketone. No activity with
	1,2-propanediol, 3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol,
	glycerol, 1-pentanol, poor activity with 1-butanol, 1-propanol,
	ethanol, and methanol <225>; #84# the enzyme exhibits broad substrate
	specificity towards aliphatic ketones, cycloalkanones, aromatic
	ketones, and ketoesters <226>; #131# the enzyme shows broad substrate
	specificity and prefers aliphatic alcohols and ketones. There are no
	large differences in the reactivities between primary and secondary
	alcohols. The enzyme produces (S)-alcohols from the corresponding
	ketones. The values of the enantiomeric excess increase with the
	increase of chain length except for the reduction of 2-hexanone. The
	highest enantioselectivity is shown with the reduction of 2-nonanone
	<239>; #132# the NAD+-dependent HvADH1 shows a preference for
	short-chain alcohols, no activity with methanol <237>; #142# broad
	substrate specificity with a preference for the reduction of ketones
	and the oxidation of secondary alcohols <138>; #123# enzyme displays a
	preference for the reduction of alicyclic, bicyclic and aromatic
	ketones and alpha-keto esters, but is poorly active on aliphatic,
	cyclic and aromatic alcohols, and shows no activity on aldehydes <219>;
	#149# enzyme reduces aldehydes to (R)-alcohols with more than 99.8%
	enantiomeric excess <243>; #150# enzyme selectively reduces the C=O
	bond of allylic aldehydes/ketones to the corresponding
	alpha,beta-unsaturated alcohols and also has the capacity of
	stereoselectively reducing aromatic ketones to (S)-enantioselective
	alcohols. The enzyme preferentially catalyzes oxidation of
	allylic/benzyl aldehydes <244>; #70# ethanol dehydrogenase activity of
	Thermoanaerobium brockii is both NAD and NADP linked, reversible, and
	not inhibited by low levels of reaction products <103>; #118,141#
	mutation at the substrate-binding site, or at a dimer interface, alters
	kinetic properties and protein oligomeric structure, active site
	flexibility is correlated with subunit interactions 20 A away <260>;
	#6# the enzyme transfers the pro-S hydrogen of [4R-(2)H]NADH and
	exhibits Prelog specificity <269>; #40# acycloNAD+ i.e. NAD+-analogue,
	where the nicotinamide ribosyl moiety has been replaced by the
	nicotinamide (2-hydroxyethoxy)methyl moiety. There is no detectable
	reduction of acycloNAD+ by secondary alcohols although these alcohols
	serve as competitive inhibitors. AcycloNAD+ converts horse liver ADH
	from a broad spectrum alcohol dehydrogenase, capable of utilizing
	either primary or secondary alcohols, into an exclusively primary
	alcohol dehydrogenase <275>; #50# bifunctional enzyme consisting of an
	N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol
	dehydrogenase (ADH). The specificity constant (kcat/Km) is 47fold
	higher for acetaldehyde reductase than that for ethanol dehydrogenase
	<279>; #152# enzyme is an alcohol dehydrogenase with additional
	activity for all-trans-retinol, reaction of EC 1.1.1.184 <272>; #154#
	enzyme shows activity as a reductase specific for (S)-acetoin, EC
	1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent
	alcohol dehydrogenase (EC 1.1.1.1) activities <271>; #159# the enzyme
	additionally catalyzes selective reduction of 3-quinuclidinone to
	(R)-3-quinuclidinol, with 84% ee and 62% conversion after 22 h <274>)
	{}
	<38,47,59,68,82,94,103,105,108,113,118,120,126,137,138,139,144,146,151
	156,169,172,180,185,188,197,204,210,211,214,215,218,219,222,223,225,226
	237,239,243,244,260,269,271,272,274,275,279>
SP	#66,80# 3-methylbutanol + NAD+ = ? + NADH <77,78>
SP	#66,80# cyclopentanol + NAD+ = ? + NADH <77,78>
SP	#66,80# D-glucitol + NAD+ = ? + NADH <77,78>
SP	#69# 2-ethylhexan-1-ol + NAD+ = 2-ethylhexanal + NADH (#69# weak
	activity <84>) <84>
SP	#70,98# ethanol + NADP+ = acetaldehyde + NADPH + H+ (#98# 8.5% of the
	activity with ethanol and NAD+ <173>) {r} <103,173>
SP	#70,98# ethanol + NADP+ = acetaldehyde + NADPH + H+ (#98# 8.5% of the
	activity with ethanol and NAD+ <173>) <103,173>
SP	#77# phenylethanol + NAD+ = phenylacetaldehyde + NADH (#77#
	R-(+)-phenylethanol and S-(-)-phenylethanol <61>) <61>
SP	#77# 2-methylbutan-1-ol + NAD+ = ? + NADH <61>
SP	#77# 3-methylbutan-2-ol + NAD+ = 3-methylbutan-2-one + NADH (#77#
	R-(-)-3-methylbutan-2-ol and S-(+)-3-methylbutan-2-ol <61>) <61>
SP	#77# hexan-2-ol + NAD+ = 2-hexanone + NADH <61>
SP	#77# trans-4-methylcyclohexanol + NAD+ = 4-methylcyclohexanone + NADH
	<61>
SP	#77# cis-4-methylcyclohexanol + NAD+ = 4-methylcyclohexanone + NADH <61>
SP	#77# heptan-2-ol + NAD+ = heptan-2-one + NADH <61>
SP	#77# heptan-4-ol + NAD+ = heptan-4-one + NADH <61>
SP	#77# R-(+)-cis-verbenol + NAD+ = ? + NADH <61>
SP	#77# R-(+)-trans-bicyclo(2.2.1)-heptanol + NAD+ =
	R-(+)-trans-bicyclo(2.2.1)-heptanal + NADH (#77#
	R-(+)-trans-bicyclo(2.2.1)-heptanol and
	S-(-)-trans-bicyclo(2.2.1)-heptanol <61>) <61>
SP	#77# S-(-)-cis-bicyclo(2.2.1)-heptanol + NAD+ =
	S-(-)-cis-bicyclo(2.2.1)-heptanal + NADH <61>
SP	#77# R-(+)-1-phenylethanol + NAD+ = 1-phenylethanone + NADH {} <61>
SP	#77# S-(-)-1-phenylethanol + NAD+ = 1-phenylethanone + NADH {} <61>
SP	#8# 3-phenyl-1-propanol + NAD+ = 3-phenyl-1-propanone + NADH {} <13,14>
SP	#8# 3-phenyl-1-propanol + NAD+ = 3-phenyl-1-propanone + NADH <13,14>
SP	#8# isobutyl alcohol + NAD+ = ? + NADH <20>
SP	#8# isopentenyl alcohol + NAD+ = isopentanone + NADH <20>
SP	#8# 16-hydroxyhexadecanoate + NAD+ = 16-oxohexadecanoic acid + NADH
	<13,14>
SP	#8# vanillyl alcohol + NAD+ = vanillin + NADH <14,16>
SP	#8# tryptophol + NAD+ = ? + NADH <14>
SP	#8# 2-deoxy-D-ribose + NAD+ = ? + NADH <14>
SP	#8# 17beta-hydroxyetiocholan-3-one + NAD+ = ethiocholan-3,17-dione +
	NADH <16>
SP	#8# phenylalaninol + NAD+ = ? + NADH <16>
SP	#8# digitose + NAD+ = ? + NADH <16>
SP	#8# 3-pyridylcarbinol + NAD+ = pyridine-3-carbaldehyde + NADH <18>
SP	#8# trans-4-(N,N-dimethylamino)-cinnamaldehyde + NADH =
	trans-4-(N,N-dimethylamino)-cinnamyl alcohol + NAD+ <19>
SP	#8# retinol + NAD+ = retinal + NADH <115>
SP	#8# 5alpha-pregnan-3beta-ol-20-one + NAD+ = 5alpha-pregnan-3,20-dione +
	NADH (#8# low activity <116>) <116>
SP	#8# isobutyramide + NAD+ = ? {r} <124>
SP	#8# 3,4-dihydro-retinol + NAD+ = 3,4-dihydro-retinal {r} <107>
SP	#8# 4-hydroxy-retinol + NAD+ = 4-oxo-retinal + NADH {r} <107>
SP	#8# 5beta-cholanic acid-3-one + NADH = 5beta-cholanic acid-3-ol + NAD+
	(#8# low activity <116>) <116>
SP	#8# 5beta-pregnan-3,20-dione + NADH = ? <116>
SP	#8# 5beta-pregnan-3beta-ol-20-one + NAD+ = 5beta-pregnan-3,20-dione +
	NADH <116>
SP	#8# hexanol + NAD+ = hexanal + NADH <119>
SP	#8# 4-hydroxynonenal + NADH + H+ = 4-hydroxynonenol + NAD+ (#8#
	substrate of isozyme ADH4 <194>) {r} <194>
SP	#8# 4-methoxy-1-naphthaldehyde + NAD+ = 4-methoxy-1-naphthyl alcohol +
	NADH + H+ (#8# substrate for class I ADH <180>) <180>
SP	#8# 4-methoxy-1-naphthaldehyde + NADH + H+ =
	4-methoxynaphthalene-1-carbaldehyde + NAD+ (#8# substrate for class I
	ADH <206>) {r} <206>
SP	#8# 6-methoxy-2-naphthaldehyde + NADH + H+ = 6-methoxy-2-naphthyl
	alcohol + NAD+ (#8# substrate for class II ADH <180>) <180>
SP	#8# 6-methoxy-2-naphthaldehyde + NADH + H+ =
	(6-methoxynaphthalen-2-yl)methanol + NAD+ (#8# substrate for class II
	ADH <206>) {r} <206>
SP	#8# m-nitrobenzaldehyde + NAD+ = m-nitrobenzyl alcohol + NADH + H+ (#8#
	substrate of class IV ADH <180>) <180>
SP	#8# n-butanol + NAD+ = butylaldehyde + NADH + H+ <180,206>
SP	#8# n-butanol + NAD+ = butylaldehyde + NADH + H+ {r} <180,206>
SP	#8# p-nitrobenzaldehyde + NADH + H+ = p-nitrobenzyl alcohol + NAD+ (#8#
	substrate of isozyme ADH4 <194>) {r} <194>
SP	#8# retinal + NADH + H+ = retinol + NAD+ (#8# substrate of isozyme ADH4
	<194>) {r} <194>
SP	#8# 4-methoxy-1-naphthaldehyde + NAD+ = 4-methoxy-1-naphthol + NADH +
	H+ (#8# fluorogenic substrate of class I and II isozymes <229>) <229>
SP	#8# 4-nitrosodimethylaniline + NAD+ = ? + NADH + H+ (#8# photometric
	assay substrate <229>) <229>
SP	#8# 6-methoxy-2-naphthaldehyde + NADH + H+ = 6-methoxy-2-naphtol + NAD+
	(#8# class II isozyme, reductive activity <229>) <229>
SP	#8,10# n-butanol + NAD+ = n-butanal + NADH <120,186>
SP	#8,10# n-butanol + NAD+ = n-butanal + NADH {r} <120,186>
SP	#8,10,40,45,46,56,70,94,95,104,111,112,118,131,141# benzyl alcohol +
	NAD+ = benzaldehyde + NADH + H+ (#95# 100% activity <156>; #46# 199% of
	the activity with 2-phenylethanol <149>; #111# 47% activity compared to
	cyclohexanol <197>; #131# i.e. phenylmethanol <239>) |#111# 154%
	activity compared to cyclohexanone <197>; #111# 178% activity compared
	to cyclohexanone <197>; #118# 33% of the activity with butan-2-ol
	<256>| <147,149,153,154,156,159,180,197,202,205,207,239,256,257,260>
SP	#8,10,40,45,46,56,70,94,95,104,111,112,118,131,141# benzyl alcohol +
	NAD+ = benzaldehyde + NADH + H+ (#95# 100% activity <156>; #46# 199% of
	the activity with 2-phenylethanol <149>; #111# 47% activity compared to
	cyclohexanol <197>; #131# i.e. phenylmethanol <239>) |#111# 154%
	activity compared to cyclohexanone <197>; #111# 178% activity compared
	to cyclohexanone <197>; #118# 33% of the activity with butan-2-ol
	<256>| {r} <147,149,153,154,156,159,180,197,202,205,207,239,256,257,260>
SP	#8,123,142# cyclohexanone + NADH + H+ = cyclohexanol + NAD+ (#142# 38%
	of the activity with acetoin <138>) <116,138,218>
SP	#8,123,142# cyclohexanone + NADH + H+ = cyclohexanol + NAD+ (#142# 38%
	of the activity with acetoin <138>) {r} <116,138,218>
SP	#8,127# 3-nitrobenzaldehyde + NADH + H+ = 3-nitrobenzyl alcohol + NAD+
	(#8# class IV isozyme, reductive activity <229>) {r} <225,229>
SP	#8,127# 3-nitrobenzaldehyde + NADH + H+ = 3-nitrobenzyl alcohol + NAD+
	(#8# class IV isozyme, reductive activity <229>) <225,229>
SP	#8,30,47,56,91,95,97,104,109,110,111,126,131# 1-butanol + NAD+ =
	butanal + NADH + H+ (#95# 30% activity compared to benzyl alcohol
	<156>; #30# 15.7% of the activity with ethanol <181>; #97# about 80% of
	activity with ethanol, ADH1 <172>; #111# 142% activity compared to
	cyclohexanol <197>; #110# 67.7% activity compared to ethanol <213>)
	<144,147,156,172,181,197,207,210,213,222,223,229,239>
SP	#8,30,47,56,91,95,97,104,109,110,111,126,131# 1-butanol + NAD+ =
	butanal + NADH + H+ (#95# 30% activity compared to benzyl alcohol
	<156>; #30# 15.7% of the activity with ethanol <181>; #97# about 80% of
	activity with ethanol, ADH1 <172>; #111# 142% activity compared to
	cyclohexanol <197>; #110# 67.7% activity compared to ethanol <213>) {r}
	<144,147,156,172,181,197,207,210,213,222,223,229,239>
SP	#8,40# 5beta-androstan-3beta-ol-17-one + NAD+ =
	5beta-androstan-3,17-dione + NADH <116>
SP	#8,40# 5beta-androstan-17beta-ol-3-one + NAD+ =
	5beta-androstan-3,17-dione + NADH (#8# low activity <116>) <116>
SP	#8,40,69,77# octan-2-ol + NAD+ = octan-2-one + NADH (#69# weak activity
	<84>; #40# (R)-2-octanol and (S)-2-octanol <31>) <16,31,61,84>
SP	#8,41# furfuryl alcohol + NAD+ = furfural + NADH (#41# activity with
	ADH I, no activity with ADH II <68>) <16,68>
SP	#8,41# furfuryl alcohol + NAD+ = furfural + NADH (#41# activity with
	ADH I, no activity with ADH II <68>) {r} <16,68>
SP	#8,9# 5alpha-androstan-17beta-ol-3-one + NADH + H+ =
	3beta,17beta-dihydroxy-5alpha-androstan + NAD+ {} <51,116>
SP	#8,9# 5alpha-androstan-17beta-ol-3-one + NADH + H+ =
	3beta,17beta-dihydroxy-5alpha-androstan + NAD+ <51,116>
SP	#8,9# m-nitrobenzaldehyde + NADH + H+ = m-nitrobenzyl alcohol + NAD+
	(#8# substrate of class IV ADH isozyme <206>) {} <49,206>
SP	#8,9# m-nitrobenzaldehyde + NADH + H+ = m-nitrobenzyl alcohol + NAD+
	(#8# substrate of class IV ADH isozyme <206>) {r} <49,206>
SP	#8,9,12,18,19,37,41,66,67,68,77,80# pentanol + NAD+ = n-pentanal + NADH
	(#41# activity with ADH I, no activity with ADH II <68>)
	<11,45,49,60,61,68,69,71,75,77,78,85>
SP	#8,9,35,68# 12-hydroxydodecanoate + NAD+ = 12-oxododecanoic acid + NADH
	(#35# oxidized at pH 10, not oxidized at pH 7.5 <47>)
	<11,14,16,47,49,53,60,95,96>
SP	#8,9,35,68# 12-hydroxydodecanoate + NAD+ = 12-oxododecanoic acid + NADH
	(#35# oxidized at pH 10, not oxidized at pH 7.5 <47>) {}
	<11,14,16,47,49,53,60,95,96>
SP	#8,9,68# octanal + NADH + H+ = octanol + NAD+ <16,49,60>
SP	#84# cycloheptanone + NADH = cycloheptanol + NAD+ <226>
SP	#84# 2-oxo-3-methylpentane + NADH = 3-methylpentan-2-ol + NAD+ <226>
SP	#84# 2-oxo-3-phenylpropane + NADH = 2-hydroxy-3-phenylpropane + NAD+
	<226>
SP	#84# 2-oxo-4-methylpentane + NADH = 4-methylpentan-2-ol + NAD+ <226>
SP	#84# 2-oxohexane + NADH = 2-hydroxyhexane + NAD+ <226>
SP	#84# 2-oxopentane + NADH = 2-pentanol + NAD+ <226>
SP	#84# 3-oxoheptane + NADH = 3-hydroxyheptane + NAD+ <226>
SP	#84# 4-phenylbutan-2-one + NADH = 4-phenylbutan-2-ol + NAD+ <226>
SP	#84# cyclooctanone + NADH = cyclooctanol + NAD+ <226>
SP	#84# cyclopentanone + NADH = cyclopentanol + NAD+ <226>
SP	#84# ethyl 3-phenyl-3-oxopropanoate + NADH = ethyl
	3-phenyl-3-hydroxypropanoate + NAD+ <226>
SP	#84# ethyl benzoylformate + NADH = ethyl (R)-mandelate + NAD+ (#84#
	enantiomeric excess of 99.9% <226>) <226>
SP	#84# ethyl pyruvate + NADH = ethyl 2-hydroxypropanoate + NAD+ <226>
SP	#84# ethyl 3-oxobutanoate + NADH = ethyl 3-hydroxybutanoate + NAD+ <226>
SP	#84# ethyl 3-oxohexanoate + NADH = ethyl 3-hydroxyhexanoate + NAD+ <226>
SP	#84# ethyl 3-oxopentanoate + NADH = ethyl 3-hydroxypentanoate + NAD+
	<226>
SP	#84# 3-methoxy-1-phenylpropan-1-one + NADH =
	3-methoxy-1-phenylpropan-1-ol + NAD+ <226>
SP	#87# 2,2,2-trichloroethanol + NAD+ = trichloroacetaldehyde + NADH + H+
	<118>
SP	#87# n-butanol + NAD+ = butanal + NADH (#87# low activity <118>) <118>
SP	#87# n-propanol + NAD+ = propionaldehyde + NADH <118>
SP	#88# 3,4-methylenedioxyphenyl acetone + NADH =
	(S)-(3,4-methylenedioxyphenyl)-2-propanol + NAD+ + H+ {} <132>
SP	#89# butanol + NAD+ = butanal + NADH <105>
SP	#9# 3beta,7alpha-dihydroxy-5beta-cholanoic acid + NAD+ = ? + NADH <51>
SP	#9# 3beta,12alpha-dihydroxy-5beta-cholanoic acid + NAD+ = ? + NADH <51>
SP	#9# 3beta,7alpha,12alpha-trihydroxy-5beta-cholanoic acid + NAD+ = ? +
	NADH <51>
SP	#9# phytol + NAD+ = phytenal + NADH + H+ <224>
SP	#9,18# 2-butene-1-ol + NAD+ = ? + NADH <49,75>
SP	#9,35,40# 3beta-hydroxy-5beta-androstan-17-one + NAD+ =
	5beta-androstan-3,17-dione + NADH (#35# catalyzed by isoenzyme BB-ADH,
	no activity with isoenzyme AA-ADH and TT-ADH <95>) {} <28,51,95>
SP	#9,35,40# 3beta-hydroxy-5beta-androstan-17-one + NAD+ =
	5beta-androstan-3,17-dione + NADH (#35# catalyzed by isoenzyme BB-ADH,
	no activity with isoenzyme AA-ADH and TT-ADH <95>) <28,51,95>
SP	#9,40# 3-oxo-5beta-androstan-17beta-ol + NADH =
	3beta,17beta-dihydroxy-5beta-androstane + NAD+ <28,42,49>
SP	#91# 2-decanol + NAD+ = 2-decanone + NADH + H+ (#91# weak activity
	<144>) {r} <144>
SP	#91# 2-nonanol + NAD+ = 2-nonanone + NADH + H+ (#91# weak activity
	<144>) {r} <144>
SP	#91# allylalcohol + NAD+ = prop-2-enal + NADH + H+ <144>
SP	#91,100,111# 2-hexanol + NAD+ = 2-hexanone + NADH + H+ (#91# weak
	activity <144>; #100# activity is 11.2fold higher than with
	(S)-N-benzyl-3-pyrrolidinol <185>; #111# 64% activity compared to
	cyclohexanol <197>) |#111# 4% activity compared to cyclohexanone <197>|
	{r} <144,185,197>
SP	#91,100,111# 2-hexanol + NAD+ = 2-hexanone + NADH + H+ (#91# weak
	activity <144>; #100# activity is 11.2fold higher than with
	(S)-N-benzyl-3-pyrrolidinol <185>; #111# 64% activity compared to
	cyclohexanol <197>) |#111# 4% activity compared to cyclohexanone <197>|
	<144,185,197>
SP	#91,111# 2-heptanol + NAD+ = 2-heptanone + NADH + H+ (#91# weak
	activity <144>; #111# 63% activity compared to cyclohexanol <197>)
	|#111# 5% activity compared to cyclohexanone <197>| {r} <144,197>
SP	#91,111,126# 2-octanol + NAD+ = 2-octanone + NADH + H+ (#91# weak
	activity <144>; #126# low activity <222>; #111# 43% activity compared
	to cyclohexanol <197>) |#111# 4% activity compared to cyclohexanone
	<197>| {r} <144,197,222>
SP	#91,92,95,97,105,109,111,126# 1-octanol + NAD+ = octanal + NADH + H+
	(#92# 33% of the activity with 2-propanol, in the reverse reaction 435%
	of the activity with phenyl trifluoromethyl ketone <137>; #95# 11%
	activity compared to benzyl alcohol <156>; #97# about 85% of activity
	with ethanol, ADH1 <172>; #111# 57% activity compared to cyclohexanol
	<197>; #105# substrate for isozyme ADH3 <214>) {r}
	<137,144,156,172,197,210,214,222>
SP	#91,92,95,97,105,109,111,126# 1-octanol + NAD+ = octanal + NADH + H+
	(#92# 33% of the activity with 2-propanol, in the reverse reaction 435%
	of the activity with phenyl trifluoromethyl ketone <137>; #95# 11%
	activity compared to benzyl alcohol <156>; #97# about 85% of activity
	with ethanol, ADH1 <172>; #111# 57% activity compared to cyclohexanol
	<197>; #105# substrate for isozyme ADH3 <214>)
	<137,144,156,172,197,210,214,222>
SP	#91,92,95,97,109,110,111,121# 1-hexanol + NAD+ = hexanal + NADH + H+
	(#92# 44% of the activity with 2-propanol, in the reverse reaction
	1029% of the activity with phenyl trifluoromethyl ketone <137>; #95#
	61% activity compared to benzyl alcohol <156>; #97# about 90% of
	activity with ethanol, ADH1 <172>; #111# 109% activity compared to
	cyclohexanol <197>; #110# 15.3% activity compared to ethanol <213>) {r}
	<137,144,156,172,197,210,213,217>
SP	#91,92,95,97,109,110,111,121# 1-hexanol + NAD+ = hexanal + NADH + H+
	(#92# 44% of the activity with 2-propanol, in the reverse reaction
	1029% of the activity with phenyl trifluoromethyl ketone <137>; #95#
	61% activity compared to benzyl alcohol <156>; #97# about 90% of
	activity with ethanol, ADH1 <172>; #111# 109% activity compared to
	cyclohexanol <197>; #110# 15.3% activity compared to ethanol <213>)
	<137,144,156,172,197,210,213,217>
SP	#91,95# 1-decanol + NAD+ = decanal + NADH + H+ (#95# 13% activity
	compared to benzyl alcohol <156>) {r} <144,156>
SP	#91,95# 1-decanol + NAD+ = decanal + NADH + H+ (#95# 13% activity
	compared to benzyl alcohol <156>) <144,156>
SP	#91,95# 1-nonanol + NAD+ = nonanal + NADH + H+ (#95# 12% activity
	compared to benzyl alcohol <156>) {r} <144,156>
SP	#91,95# 1-nonanol + NAD+ = nonanal + NADH + H+ (#95# 12% activity
	compared to benzyl alcohol <156>) <144,156>
SP	#91,95,109,111# 1-heptanol + NAD+ = heptanal + NADH + H+ (#95# 25%
	activity compared to benzyl alcohol <156>; #111# 80% activity compared
	to cyclohexanol <197>) {r} <144,156,197,210>
SP	#91,95,109,111# 1-heptanol + NAD+ = heptanal + NADH + H+ (#95# 25%
	activity compared to benzyl alcohol <156>; #111# 80% activity compared
	to cyclohexanol <197>) <144,156,197,210>
SP	#91,95,97,109,110,111,126# 1-pentanol + NAD+ = pentanal + NADH + H+
	(#95# 152% activity compared to benzyl alcohol <156>; #97# about 85% of
	activity with ethanol, ADH1 <172>; #111# 121% activity compared to
	cyclohexanol <197>; #110# 19.1% activity compared to ethanol <213>) {r}
	<144,156,172,197,210,213,222>
SP	#91,95,97,109,110,111,126# 1-pentanol + NAD+ = pentanal + NADH + H+
	(#95# 152% activity compared to benzyl alcohol <156>; #97# about 85% of
	activity with ethanol, ADH1 <172>; #111# 121% activity compared to
	cyclohexanol <197>; #110# 19.1% activity compared to ethanol <213>)
	<144,156,172,197,210,213,222>
SP	#91,97,99,100,111,131# 2-butanol + NAD+ = 2-butanone + NADH + H+ (#91#
	weak activity <144>; #97# about 25% of activity with ethanol, ADH1
	<172>; #100# activity is 3.7fold higher than with
	(S)-N-benzyl-3-pyrrolidinol <185>; #111# 39% activity compared to
	cyclohexanol <197>) |#111# 4% activity compared to cyclohexanone <197>|
	<144,171,172,185,197,239>
SP	#91,97,99,100,111,131# 2-butanol + NAD+ = 2-butanone + NADH + H+ (#91#
	weak activity <144>; #97# about 25% of activity with ethanol, ADH1
	<172>; #100# activity is 3.7fold higher than with
	(S)-N-benzyl-3-pyrrolidinol <185>; #111# 39% activity compared to
	cyclohexanol <197>) |#111# 4% activity compared to cyclohexanone <197>|
	{r} <144,171,172,185,197,239>
SP	#92# (R)-2-heptanol + NAD+ = 2-heptanone + NADH + H+ (#92# 2469% of the
	activity with 2-propanol <137>) {r} <137>
SP	#92# (R)-2-hexanol + NAD+ = 2-hexanone + NADH + H+ (#92# 1906% of the
	activity with 2-propanol <137>) {r} <137>
SP	#92# (S)-2-heptanol + NAD+ = 2-heptanone + NADH + H+ (#92# 331% of the
	activity with 2-propanol <137>) {r} <137>
SP	#92# (S)-2-hexanol + NAD+ = 2-hexanone + NADH + H+ (#92# 38% of the
	activity with 2-propanol <137>) {r} <137>
SP	#92# 1,1-dichloroacetone + NADH + H+ = 1,1-dichloropropan-2-ol + NADH
	(#92# 1078% of the activity with phenyl trifluoromethyl ketone <137>)
	<137>
SP	#92# 1-heptanol + NAD+ = heptanol + NADH + H+ (#92# 56% of the activity
	with 2-propanol, in the reverse reaction 755% of the activity with
	phenyl trifluoromethyl ketone <137>) {r} <137>
SP	#92# 1-phenyl-3-butanone + NADH + H+ = 1-phenylbutan-3-ol + NAD+ (#92#
	353% of the activity with phenyl trifluoromethyl ketone <137>) <137>
SP	#92# 2,3'-dichloroacetophenone + NADH + H+ =
	1-(2,3-dichlorophenyl)ethanol + NAD+ (#92# 67% of the activity with
	phenyl trifluoromethyl ketone <137>) <137>
SP	#92# 2-heptanone + NADH + H+ = (R)-2-heptanol + NAD+ (#92# 229% of the
	activity with phenyl trifluoromethyl ketone <137>) |#92# 99%
	enantiomeric excess <137>| <137>
SP	#92# 3',4'-dimethoxyphenylacetone + NADH + H+ =
	1-(3,4-dimethoxyphenyl)propan-2-ol + NAD+ (#92# 24% of the activity
	with phenyl trifluoromethyl ketone <137>) <137>
SP	#92# 3'-bromoacetophenone + NADH + H+ = 1-(3-bromophenyl)ethanol + NAD+
	(#92# 151% of the activity with phenyl trifluoromethyl ketone <137>)
	<137>
SP	#92# 3'-chloroacetophenone + NADH + H+ = 1-(3-chlorophenyl)ethanol +
	NAD+ (#92# 70% of the activity with phenyl trifluoromethyl ketone
	<137>) <137>
SP	#92# 3'-methoxyacetophenone + NADH + H+ = 1-(3-methoxyphenyl)ethanol +
	NAD+ (#92# 51% of the activity with phenyl trifluoromethyl ketone
	<137>) <137>
SP	#92# 3-chloro-2-butanone + NADH + H+ = 3-chlorobutan-2-ol + NAD+ (#92#
	151% of the activity with phenyl trifluoromethyl ketone <137>) <137>
SP	#92# 3-heptanol + NAD+ = 3-heptanone + NADH + H+ (#92# 93% of the
	activity with 2-propanol <137>) {r} <137>
SP	#92# 3-phenylpropionaldehyde + NADH = 3-phenylpropan-1-ol + NAD+ (#92#
	1218% of the activity with phenyl trifluoromethyl ketone <137>) <137>
SP	#92# 4'-bromoacetophenone + NADH + H+ = 1-(4-bromophenyl)ethanol + NAD+
	(#92# 77% of the activity with phenyl trifluoromethyl ketone <137>)
	<137>
SP	#92# 4'-chloroacetophenone + NADH + H+ = 1-(4-chlorophenyl)ethanol +
	NAD+ (#92# 60% of the activity with phenyl trifluoromethyl ketone
	<137>) <137>
SP	#92# 4-hydroxy-2-butanone + NADH + H+ = 2,4-dihydroxybutane + NAD+
	(#92# 26% of the activity with phenyl trifluoromethyl ketone <137>)
	<137>
SP	#92# acetophenone + NADH + H+ = (R)-1-phenylethanol + NAD+ (#92# 6% of
	the activity with phenyl trifluoromethyl ketone, in the reverse
	reaction 87% of the activity with 2-propanol <137>) |#92# 99%
	enantiomeric excess <137>| <137>
SP	#92# butanal + NADH = 1-butanol + NAD+ + H+ (#92# % of the activity
	with phenyl trifluoromethyl ketone <137>) {ir} <137>
SP	#92# ethyl 3-methyl-2-oxobutyrate + NADH + H+ =
	ethyl-2-hydroxy-3-methylbutyrate + NAD+ (#92# 33% of the activity with
	phenyl trifluoromethyl ketone <137>) <137>
SP	#92# ethyl 3-oxobutanoate + NADH + H+ = ethyl 3-hydroxybutanoate + NAD+
	(#92# 309% of the activity with phenyl trifluoromethyl ketone <137>)
	<137>
SP	#92# ethyl 4-bromo-3-oxobutanoate + NADH + H+ = ethyl
	4-bromo-3-hydroxybutanoate (#92# 511% of the activity with phenyl
	trifluoromethyl ketone <137>) <137>
SP	#92# ethyl 4-chloro-3-oxobutanoate + NADH + H+ = ethyl
	4-chloro-3-hydroxybutanoate + NAD+ (#92# 809% of the activity with
	phenyl trifluoromethyl ketone <137>) <137>
SP	#92# ethyl pyruvate + NADH + H+ = ethyl 2-hydroxypropanoate + NAD+
	(#92# 488% of the activity with phenyl trifluoromethyl ketone <137>)
	<137>
SP	#92# methyl 3-oxobutanoate + NADH + H+ = methyl 3-hydroxybutanoate +
	NAD+ (#92# 130% of the activity with phenyl trifluoromethyl ketone
	<137>) <137>
SP	#92# methyl 4-bromo-3-oxobutanoate + NADH + H+ = methyl
	4-bromo-3-hydroxybutanoate + NAD+ (#92# 164% of the activity with
	phenyl trifluoromethyl ketone <137>) <137>
SP	#92# pentanal + NADH = 1-pentanol + NAD+ + H+ (#92# 132% of the
	activity with phenyl trifluoromethyl ketone, in the reverse reaction 5%
	of the activity with 2-propanol <137>) <137>
SP	#92# phenyl trifluoromethyl ketone + NADH + H+ =
	(S)-1-phenyltrifluoroethanol + NAD+ |#92# more than 99% enantiomeric
	excess <137>| <137>
SP	#92# tert-butyl 3-oxobutanoate + NADH + H+ = tert butyl
	3-hydroxybutanoate + NAD+ (#92# 568% of the activity with phenyl
	trifluoromethyl ketone <137>) <137>
SP	#92,104# trans-cinnamaldehyde + NADH + H+ = cinnamyl alcohol + NAD+
	(#92# % of the activity with phenyl trifluoromethyl ketone <137>) {r}
	<137,207>
SP	#92,104# trans-cinnamaldehyde + NADH + H+ = cinnamyl alcohol + NAD+
	(#92# % of the activity with phenyl trifluoromethyl ketone <137>)
	<137,207>
SP	#93# iso-propanol + NAD+ = isopropanal + NADH + H+ <162>
SP	#93,99# n-propanol + NAD+ = propanal + NADH + H+ <162,171>
SP	#93,99# n-propanol + NAD+ = propanal + NADH + H+ {r} <162,171>
SP	#95# 4-nitrobenzyl alcohol + NAD+ = 4-nitrobenzaldehyde + NADH + H+
	(#95# 94% activity compared to benzyl alcohol <156>) <156>
SP	#95# choline + NAD+ = ? + NADH + H+ (#95# 3% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# decyl aldehyde + NADH + H+ = 1-decanol + NAD+ (#95# 21% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# heptaldehyde + NADH + H+ = ? + NAD+ (#95# 33% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# hexaldehyde + NADH + H+ = 1-hexanol + NAD+ (#95# 7% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# hydrocinnamaldehyde + NADH + H+ = hydrocinnamyl alcohol + NAD+
	(#95# 12% activity compared to benzyl alcohol <156>) {r} <156>
SP	#95# hydrocinnamyl alcohol + NAD+ = hydrocinnamaldehyde + NADH + H+
	(#95# 31% activity compared to benzyl alcohol <156>) {r} <156>
SP	#95# nonyl aldehyde + NADH + H+ = 1-nonanol + NAD+ (#95# 25% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# nonylphenol polyethoxylate 9 + NAD+ = ? + NADH (#95# 7% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# octyl aldehyde + NADH + H+ = 1-octanol + NAD+ (#95# 29% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# octylphenol polyethoxylate 2 + NAD+ = ? + NADH (#95# 59% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# octylphenol polyethoxylate 8 + NAD+ = ? + NADH (#95# 7% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# polyoxyethylene 8 decyl ether + NAD+ = ? + NADH (#95# 12% activity
	compared to benzyl alcohol <156>) <156>
SP	#95# Triton X-100 + NAD+ = ? + NADH (#95# 7% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# Triton X-114 + NAD+ = ? + NADH (#95# 3% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# Triton X-165 + NAD+ = ? + NADH (#95# 24% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# Triton X-35 + NAD+ = ? + NADH (#95# 43% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# Triton X-405 + NAD+ = ? + NADH (#95# 19% activity compared to
	benzyl alcohol <156>) <156>
SP	#95# Triton X-45 + NAD+ = ? + NADH (#95# 7% activity compared to benzyl
	alcohol <156>) <156>
SP	#96# acetophenone + NADPH + H+ = 1-phenylethanol + NADP+ (#96# 5.1% of
	the activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# 2-butanone + NADPH + H+ = butan-2-ol + NADP+ (#96# 12.1% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# 2-heptanone + NADPH + H+ = heptan-2-ol + NADP+ (#96# 6.8% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# 2-hexanone + NADPH + H+ = hexan-2-ol + NADP+ (#96# 5.9% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# 2-hydroxyacetophenone + NADH + H+ = (S)-1-phenyl-1,2-ethanediol +
	NAD+ (#96# 2.4% of the activity with NADPH <168>) <168>
SP	#96# 2-hydroxyacetophenone + NADPH + H+ = (S)-1-phenyl-1,2-ethanediol +
	NADP+ <168>
SP	#96# 2-octanone + NADPH + H+ = octan-2-ol + NADP+ (#96# 11.9% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# 2-pentanone + NADPH + H+ = pentan-2-ol + NADP+ (#96# 11.9% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# 3-pentanone + NADPH + H+ = pentan-3-ol + NADP+ (#96# 7.1% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# acetone + NADPH + H+ = propan-2-ol + NADP+ (#96# 14.7% of the
	activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# benzoylformic acid + NADPH + H+ = mandelate + NADP+ (#96# 2.4% of
	the activity with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# ethyl 4-chloroacetoacetate + NADPH = ? (#96# activity is 1.48fold
	higher than with 2-hydroxyacetophenone and NADPH <168>) <168>
SP	#96# ethyl trifluoroacetoacetate + NADPH + H+ =
	1-ethoxy-2,2,2-trifluoroethanol + NADP+ (#96# 4.3% of the activity with
	2-hydroxyacetophenone and NADPH <168>) <168>
SP	#98# 2,3-butanediol + H2O = ? <173>
SP	#98# 2-aminoethanol + NAD+ = ? <173>
SP	#99# 2-propanol + NAD+ = propanone + NADH + H+ {r} <171>
SP	#99# n-pentanol + NAD+ = pentanal + NADH + H+ <171>
SP	#99# n-butanal + NADH + H+ = n-butanol + NAD+ <171>
SP	#99# n-butanol + NAD+ = n-butanal + NADH + H+ <171>

TURNOVER_NUMBER
TN	#10# 0.73 {propanal}  (#10# pH 7.0, 30°C <285>) <285>
TN	#10# 1.28 {formaldehyde}  (#10# pH 7.0, 30°C <285>) <285>
TN	#10# 143 {ethanol}  (#10# in 50 mM Tris-HCl, pH 8.0 at 25°C <209>)
	<209>
TN	#10# 1.58 {furfural}  (#10# pH 7.0, 30°C <285>) <285>
TN	#10# 1.99 {Butanal}  (#10# pH 7.0, 30°C <285>) <285>
TN	#10# 251.3 {ethanol}  (#10# 10°C, pH 9.0 <144>) <144>
TN	#10# 432.3 {ethanol}  (#10# 20°C, pH 9.0 <144>) <144>
TN	#10# 786.1 {ethanol}  (#10# 30°C, pH 9.0 <144>) <144>
TN	#10# 895.4 {ethanol}  (#10# 40°C, pH 9.0 <144>) <144>
TN	#10# 18.65 {glycolaldehyde}  (#10# pH 7.0, 30°C <285>) <285>
TN	#104# 0.52 {NAD+}  (#104# mutant enzyme W95L, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.1 {(R)-2-pentanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1 {(R)-2-butanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.5 {3-Pentanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 2.6 {(S)-2-pentanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.6 {1-Heptanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.6 {2-ethoxyethanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 2 {1-Hexanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 2.1 {trans-cinnamaldehyde}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.21 {trans-cinnamaldehyde}  (#104# mutant enzyme W95L,, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.53 {1-Pentanol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 3.1 {ethanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 3.1 {1-butanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.7 {(R)-2-butanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 2.9 {4-methoxybenzyl alcohol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 21 {NAD+}  (#104# Km above 50 mM, mutant enzyme W95L/N249Y, in
	0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 2.5 {1-propanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 2.5 {1-Pentanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.82 {Isobutyraldehyde}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 16.3 {1-Pentanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 20 {benzyl alcohol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 4.8 {(S)-2-butanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.9 {(R)-2-pentanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 13.1 {benzaldehyde}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 15.1 {1-butanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 16.8 {4-methoxybenzyl alcohol}  (#104# mutant enzyme W95L/N249Y,
	in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 18.1 {Isobutyraldehyde}  (#104# mutant enzyme W95L/N249Y, in 0.1
	M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.38 {NADH}  (#104# mutant enzyme W95L, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 1.2 {(S)-2-butanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 29 {Isobutyraldehyde}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.37 {4-methoxybenzyl alcohol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 12.4 {Cyclohexanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.35 {benzyl alcohol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 6.7 {(S)-2-pentanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 13.3 {1-Hexanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.36 {benzaldehyde}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.36 {Butyraldehyde}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.42 {1-Hexanol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 11.9 {1-Heptanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 18.9 {trans-cinnamaldehyde}  (#104# mutant enzyme W95L/N249Y, in
	0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 4.1 {ethanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 34.8 {NADH}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 19.7 {Butyraldehyde}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>; #104# wild type enzyme,
	in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 15.7 {1-propanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#104# 0.51 {1-Heptanol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
TN	#113# 43.9 {NADP+}  (#113# cosubstrate ethanol, pH 8.0, 60°C <215>)
	<215>
TN	#113# 638.7 {ethanol}  (#113# cosubstrate NAD+, pH 8.0, 60°C <215>)
	<215>
TN	#113# 404.8 {acetaldehyde}  (#113# cosubstrate NADH, pH 8.0, 60°C
	<215>) <215>
TN	#113# 443.1 {NAD+}  (#113# cosubstrate ethanol, pH 8.0, 60°C <215>)
	<215>
TN	#113# 1646 {NADH}  (#113# cosubstrate acetaldehyde, pH 8.0, 60°C
	<215>) <215>
TN	#114# 38.5 {NAD+}  (#114# cosubstrate 1-octanol, pH 8.0, 60°C <215>)
	<215>
TN	#114# 138.1 {acetaldehyde}  (#114# cosubstrate NADPH, pH 8.0, 60°C
	<215>) <215>
TN	#114# 283.1 {NADP+}  (#114# cosubstrate 1-octanol, pH 8.0, 60°C <215>)
	<215>
TN	#114# 4808 {NADPH}  (#114# cosubstrate octanal, pH 8.0, 60°C <215>)
	<215>
TN	#114# 136.2 {ethanol}  (#114# cosubstrate NADP+, pH 8.0, 60°C <215>)
	<215>
TN	#114# 260.7 {1-Octanol}  (#114# cosubstrate NADP+, pH 8.0, 60°C <215>)
	<215>
TN	#114# 518.4 {octanal}  (#114# cosubstrate NADPH, pH 8.0, 60°C <215>)
	<215>
TN	#118# 8 {NAD+}  (#118# wild-type, 30°C, pH not specified in the
	publication <257>) <257>
TN	#118# 3 {NAD+}  (#118# mutant W49F/W87F, 30°C, pH not specified in the
	publication <257>) <257>
TN	#118# 5.5 {benzyl alcohol}  (#118# mutant W87A, pH 7.0, 30°C <260>)
	<260>
TN	#118# 2.5 {NAD+}  (#118# mutant Y25A/W49F/W167Y, 30°C, pH not
	specified in the publication <257>; #118# mutant Y25A/W49F/W87F/V260A,
	30°C, pH not specified in the publication <257>) <257>
TN	#118# 24.9 {benzyl alcohol}  (#118# wild-type, pH 7.0, 30°C <260>)
	<260>
TN	#118# 14 {benzyl alcohol}  (#118# mutant Y25A, pH 7.0, 30°C <260>)
	<260>
TN	#118# 1.9 {NAD+}  (#118# mutant V260A, 30°C, pH not specified in the
	publication <257>; #118# mutant Y25A/W49F/W167Y/V260A, 30°C, pH not
	specified in the publication <257>) <257>
TN	#118# 195 {n-butanol}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
TN	#118# 6.3 {NAD+}  (#118# mutant Y25A/W49F/W87F, 30°C, pH not specified
	in the publication <257>) <257>
TN	#118# 5.1 {NAD+}  (#118# mutant Y25A, 30°C, pH not specified in the
	publication <257>) <257>
TN	#118# 365 {ethanol}  (#118# mutant C257L, pH 8.0, 60°C <246>) <246>
TN	#118# 308 {12-oxolauric acid methyl ester}  (#118# wild-type, pH 8.0,
	60°C <246>) <246>
TN	#118# 305 {ethanol}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
TN	#118# 27.6 {12-hydroxylauric acid methyl ester}  (#118# wild-type, pH
	8.0, 60°C <246>) <246>
TN	#118# 34.2 {NAD+}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
TN	#118# 34.3 {12-hydroxylauric acid methyl ester}  (#118# mutant C257L,
	pH 8.0, 60°C <246>) <246>
TN	#118# 931 {Butyraldehyde}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
TN	#118# 681 {acetaldehyde}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
TN	#118# 326 {NADH}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
TN	#118,154# 1 {NAD+}  (#118# mutant W49F/W87F/V260A, 30°C, pH not
	specified in the publication <257>; #154# cosubstrate butan-1-ol, pH
	7.0, 30°C <271>) <257,271>
TN	#122# 3.8 {3-methylcyclohexanone}  (#122# 65°C, pH 5.5 <219>) <219>
TN	#122# 3.1 {1-phenyl-1,2-propanedione}  (#122# 65°C, pH 5.5 <219>) <219>
TN	#122# 10 {2,2,2-trifluoroacetophenone}  (#122# 65°C, pH 5.5 <219>)
	<219>
TN	#122# 0.98 {cis-decahydro-1-naphthol}  (#122# 65°C, pH 8.0 <219>) <219>
TN	#122# 6.2 {methyl benzoylformate}  (#122# 65°C, pH 5.5 <219>) <219>
TN	#122# 2.35 {ethyl benzoylformate}  (#122# 65°C, pH 5.5 <219>) <219>
TN	#122,123# 2-8 {NADH}  (#123# pH 5.5, 65°C <219>; #122# 65°C, pH 5.5
	<219>) <219>
TN	#122,123# 3.7 {NAD+}  (#123# pH 8.0, 65°C <219>; #122# 65°C, pH 8.0
	<219>) <219>
TN	#122,123# 2.1 {(S)-alpha-tetralol}  (#123# pH 8.0, 65°C <219>; #122#
	65°C, pH 8.0 <219>) <219>
TN	#122,123# 22 {isatin}  (#123# pH 5.5, 65°C <219>; #122# 65°C, pH 5.5
	<219>) <219>
TN	#122,123# 9.2 {methyl o-chlorobenzoylformate}  (#123# pH 5.5, 65°C
	<219>; #122# 65°C, pH 5.5 <219>) <219>
TN	#122,123# 13.5 {(R)-alpha-tetralol}  (#123# pH 8.0, 65°C <219>; #122#
	65°C, pH 8.0 <219>) <219>
TN	#122,123# 4.4 {cycloheptanol}  (#123# pH 8.0, 65°C <219>; #122# 65°C,
	pH 8.0 <219>) <219>
TN	#122,123# 7.1 {(R)-1-indanol}  (#123# pH 8.0, 65°C <219>; #122# 65°C,
	pH 8.0 <219>) <219>
TN	#122,123# 13.7 {(S)-1-indanol}  (#123# pH 8.0, 65°C <219>; #122#
	65°C, pH 8.0 <219>) <219>
TN	#123# 7 {cycloheptanol}  (#123# 65°C, pH 10.5 <218>) <218>
TN	#123# 1.6 {benzil}  (#123# 65°C, pH 5.0 <218>) <218>
TN	#123# 3.2 {2',3',4',5',6'-pentafluoroacetophenone}  (#123# 65°C, pH
	5.0 <218>) <218>
TN	#123# 1.7 {2,2,2-trifluoroacetophenone}  (#123# 65°C, pH 5.0 <218>)
	<218>
TN	#123# 0.65 {2,2-dichloroacetophenone}  (#123# 65°C, pH 5.0 <218>) <218>
TN	#123# 1.9 {ethyl benzoylformate}  (#123# 65°C, pH 5.0 <218>) <218>
TN	#123# 9.6 {tetralin-1-ol}  (#123# 65°C, pH 10.5 <218>) <218>
TN	#123# 5.3 {1-phenyl-1,2-propanedione}  (#123# 65°C, pH 5.0 <218>) <218>
TN	#123# 26 {ethyl 3-methyl-2-oxobutyrate}  (#123# 65°C, pH 5.0 <218>)
	<218>
TN	#123# 26.2 {NADH}  (#123# 65°C, pH 5.0 <218>) <218>
TN	#123# 6.2 {1-Indanol}  (#123# 65°C, pH 10.5 <218>) <218>
TN	#123# 19.3 {NAD+}  (#123# 65°C, pH 10.5 <218>) <218>
TN	#123# 16.6 {isoborneol}  (#123# 65°C, pH 10.5 <218>) <218>
TN	#126# 3000 {ethanol}  (#126# pH 9.0, 22°C, recombinant enzyme <222>)
	<222>
TN	#126# 3500 {acetaldehyde}  (#126# pH 6.0, 22°C, recombinant enzyme
	<222>) <222>
TN	#13# 55 {cinnamaldehyde}  (#13# pH 7.7, 60°C <234>) <234>
TN	#13# 33 {NAD+}  (#13# pH 7.7, 60°C <234>) <234>
TN	#13# 43 {NADH}  (#13# pH 7.7, 60°C <234>) <234>
TN	#13# 43 {cinnamyl alcohol}  (#13# pH 7.7, 60°C <234>) <234>
TN	#13# 287 {2-propanol}  (#13# pH 7.7, 60°C <234>) <234>
TN	#130# 3.17 {Octanol}  (#130# pH and temperature not specified in the
	publication <227>) <227>
TN	#131# 0.41 {NADH}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.41 {1-butanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.52 {Cyclohexanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.26 {1-propanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.4 {NAD+}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.4 {2-decanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.24 {2-propanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.73 {2-Heptanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.74 {2-Octanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.77 {2-Pentanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.6 {4-methoxybenzyl alcohol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.6 {2-Pentanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.45 {1-Pentanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 1.27 {cyclohexanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.37 {1-Hexanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 1.02 {benzyl alcohol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 1.08 {2-Hexanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.071 {4-methoxyphenylacetone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 1.22 {benzaldehyde}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.48 {2-butanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.23 {ethanol}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.7-1 {2-nonanone}  (#131# pH 8.0, 60°C <239>) <239>
TN	#131# 0.072 {tert-butyl acetoacetate}  (#131# pH 8.0, 60°C <239>) <239>
TN	#135# 142 {ethanol}  (#135# pH 7.0, temperature not specified in the
	publication <252>) <252>
TN	#135# 283 {acetaldehyde}  (#135# pH 7.0, temperature not specified in
	the publication <252>) <252>
TN	#136# 4.5 {ethanol}  (#136# pH 7.0, temperature not specified in the
	publication <252>) <252>
TN	#136# 53 {acetaldehyde}  (#136# pH 7.0, temperature not specified in
	the publication <252>) <252>
TN	#137# 33 {ethanol}  (#137# pH 7.0, temperature not specified in the
	publication <252>) <252>
TN	#138# 158 {ethanol}  (#138# pH 7.0, temperature not specified in the
	publication <252>) <252>
TN	#141# 3.8 {benzyl alcohol}  (#141# mutant A25Y, pH 7.0, 30°C <260>)
	<260>
TN	#141# 6.9 {benzyl alcohol}  (#141# wild-type, pH 7.0, 30°C <260>) <260>
TN	#148# 350 {acetaldehyde}  (#148# alcohol dehydrogenase domain, 60°C,
	pH 6.0, presence of 0.1 mM Zn2+ <241>) <241>
TN	#148# 83 {acetaldehyde}  (#148# wild-type, 60°C, pH 6.0, presence of
	0.1 mM Zn2+ <241>) <241>
TN	#149# 30 {NADP+}  (#149# cosubstrate 2,3-butanediol, pH 9.0, 70°C
	<243>) <243>
TN	#149# 17.3 {NADH}  (#149# cosubstrate acetoin, pH 6.0, 70°C <243>)
	<243>
TN	#149# 15.6 {NADH}  (#149# cosubstrate acetoin, pH 6.0, 70°C <243>)
	<243>
TN	#149# 10.5 {NADP+}  (#149# cosubstrate 1-phenylethanol, pH 9.0, 70°C
	<243>) <243>
TN	#149# 10.4 {NAD+}  (#149# cosubstrate 1-phenylethanol, pH 9.0, 70°C
	<243>) <243>
TN	#149# 43.8 {2,3-Butanediol}  (#149# pH 9.0, 70°C <243>) <243>
TN	#149# 13.7 {acetoin}  (#149# pH 6.0, 70°C <243>) <243>
TN	#149# 30.8 {NAD+}  (#149# cosubstrate 2,3-butanediol, pH 9.0, 70°C
	<243>) <243>
TN	#149# 35.7 {1-phenylethanol}  (#149# pH 9.0, 70°C <243>) <243>
TN	#150# 433 {NADPH}  (#150# pH 6.5, 65°C <244>) <244>
TN	#150# 360 {benzaldehyde}  (#150# pH 6.5, 65°C <244>) <244>
TN	#150# 194 {NADP+}  (#150# pH 8.0, 55°C <244>) <244>
TN	#150# 101 {(2E)-but-2-en-1-ol}  (#150# pH 8.0, 55°C <244>) <244>
TN	#150# 405 {(2E)-but-2-enal}  (#150# pH 6.5, 65°C <244>) <244>
TN	#150# 93.3 {benzyl alcohol}  (#150# pH 8.0, 55°C <244>) <244>
TN	#154# 2 {butan-1-ol}  (#154# cosubstrate NAD+, pH 7.0, 30°C <271>)
	<271>
TN	#154# 153 {NADH}  (#154# cosubstrate butanal, pH 7.0, 30°C <271>) <271>
TN	#154# 102 {Butanal}  (#154# cosubstrate NADH, pH 7.0, 30°C <271>) <271>
TN	#26# 4.5 {ethylene glycol}  <129>
TN	#30# 0.3 {acetaldehyde}  (#30# 40°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl
	<181>) <181>
TN	#30# 5.4 {acetaldehyde}  (#30# 70°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl
	<181>) <181>
TN	#30# 8.2 {ethanol}  (#30# 70°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl
	<181>) <181>
TN	#30,78# 0.4 {ethanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>;
	#30# 40°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl <181>) <24,181>
TN	#35# 8 {ethanol}  <47>
TN	#35# 1.3 {all-trans retinol}  (#35# isoenzyme TT-ADH <95>) <47,95>
TN	#35# 2.2 {12-hydroxydodecanoate}  (#35# isoenzyme BB-ADH <95>) <95>
TN	#35# 2.8 {n-Hexanol}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 3 {methylcrotonyl alcohol}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 1.03 {12-hydroxydodecanoate}  (#35# isoenzyme TT-ADH <95>) <95>
TN	#35# 1.37 {benzyl alcohol}  <47>
TN	#35# 1.9 {all-trans retinol}  (#35# isoenzyme BB-ADH <95>) <95>
TN	#35# 2.83 {ethanol}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 7.5 {1-butanol}  <47>
TN	#35# 2.4 {Cyclohexanol}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 8.5 {Cyclohexanol}  (#35# isoenzyme TT-ADH <95>) <95>
TN	#35# 3.33 {n-butanol}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 0.35 {all-trans retinol}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 8.58 {methylcrotonyl alcohol}  (#35# isoenzyme TT-ADH <95>) <95>
TN	#35# 2.03 {Cyclohexanol}  <47>
TN	#35# 2.35 {n-Hexanol}  (#35# isoenzyme BB-ADH <95>) <95>
TN	#35# 2.43 {12-hydroxydodecanoate}  <47>
TN	#35# 2.58 {n-butanol}  (#35# isoenzymee BB-ADH <95>) <95>
TN	#35# 2.63 {methylcrotonyl alcohol}  (#35# isoenzyme BB-ADH <95>) <95>
TN	#35# 2.77 {12-hydroxydodecanoate}  (#35# isoenzyme AA-ADH <95>) <95>
TN	#35# 3.03 {1-Hexanol}  <47>
TN	#35# 3.38 {ethanol}  (#35# isoenzyme BB-ADH <95>) <95>
TN	#35# 4.08 {n-Hexanol}  (#35# isoenzyme TT-ADH <95>) <95>
TN	#35# 4.75 {2-butanol}  <47>
TN	#35# 7.18 {n-butanol}  (#35# isoenzyme TT-ADH <95>) <95>
TN	#35# 7.75 {NAD+}  (#35# oxidation of ethanol <47>) <47>
TN	#35# 9.58 {ethanol}  (#35# isoenzyme TT-ADH <95>) <95>
TN	#4,5,8,40,74# -999 {more}  (#8# turnover-numbers for the class I
	isoenzymes with the substrates ethanol, methanol, ethylene glycol,
	benzyl alcohol, octanol, cyclohexanol and 16-hydroxyhexadecanoic acid
	<13>; #40# Km-values of active-site Co(II)substituted enzyme <31>;
	#4,74# kinetics of ethanol oxidation <63>; #5# kcat for isozymes ADH1,
	and ADH4 for all retinoid substrates in forward and reverse reaction
	<119>; #8# kcat for isozymes ADH1B1, ADH1B2, and ADH4 for all retinoid
	substrates in forward and reverse reaction <119>; #5# effects of
	tert-butanol, butyramide, valeramide and capronamide on turnover-number
	of ethanol <141>) <13,28,31,63,119,141>
TN	#40# 0.99 {hexyl alcohol}  <42>
TN	#40# 1 {(S)-2-butanol}  <31>
TN	#40# 0.9 {5beta-Pregnan-21-ol-3,20-dione hemisuccinate}  <42>
TN	#40# 2 {(R)-2-butanol}  <31>
TN	#40# 2.05 {3-oxo-5beta-androstan-17beta-ol}  <42>
TN	#40# 0.24 {p-nitrophenyl octanoate}  <39>
TN	#40# 2.5 {all-trans-retinal}  (#40# reduction with NADH <93>) <93>
TN	#40# 1.17 {Propyl alcohol}  <42>
TN	#40# 0.78 {benzyl alcohol}  <42>
TN	#40# 0.87 {(S)-2-pentanol}  <31>
TN	#40# 1.01 {(R)-2-pentanol}  <31>
TN	#40# 0.08 {3-methyl-1-butanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 5.8 {propan-2-ol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 0.12 {2-butanone}  <31>
TN	#40# 0.025 {9-cis-retinol}  (#40# oxidation with NAD+ <93>) <93>
TN	#40# 1.27 {ethanol}  <42>
TN	#40# 1.55 {all-trans-retinol}  (#40# oxidation with NAD+ <93>) <93>
TN	#40# 5.9 {cyclohexanone}  <42>
TN	#40# 6.7 {4-Methyl-1-pentanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 0.018 {13-cis-retinal}  (#40# reduction with NADH <93>) <93>
TN	#40# 0.018 {13-cis-retinol}  (#40# oxidation with NAD+ <93>) <93>
TN	#40# 0.36 {3-Pentanone}  <31>
TN	#40# 0.021 {11-cis-retinal}  (#40# reduction with NADH <93>) <93>
TN	#40# 133 {cinnamyl alcohol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 0.053 {(R)-2-octanol}  <31>
TN	#40# 308 {ethanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 98 {cinnamyl alcohol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 102 {ethanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 11.9 {butan-2-ol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 0.31 {butan-2-ol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 29.6 {Hexanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 1.52 {(S)-2-octanol}  <31>
TN	#40# 118 {butanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 18.6 {4-Methyl-1-pentanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 23.9 {Hexanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 0.022 {all-trans-retinal}  (#40# oxidation with NAD+ <93>) <93>
TN	#40# 0.022 {11-cis-retinol}  (#40# oxidation with NAD+ <93>) <93>
TN	#40# 123 {ethanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 0.27 {3-methyl-1-butanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 0.33 {acetone}  <31>
TN	#40# 53.1 {propan-2-ol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#40# 28.7 {Propanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 56.6 {hexaldehyde}  <42>
TN	#40# 0.023 {9-cis-retinal}  (#40# reduction with NADH <93>) <93>
TN	#40# 0.0713 {2-Pentanone}  <31>
TN	#40# 0.58 {Isopropanol}  <31>
TN	#40# 0.94 {Butyl alcohol}  <42>
TN	#40# 2.26 {3-Pentanol}  <31>
TN	#40# 18.4 {Pentanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 29.5 {benzaldehyde}  <42>
TN	#40# 31.8 {acetaldehyde}  <42>
TN	#40# 32.7 {butanol}  (#40# mutant enzyme W54L <92>) <92>
TN	#40# 35.4 {Butyraldehyde}  <42>
TN	#40# 41.9 {propionaldehyde}  <42>
TN	#40# 56.2 {Pentanol}  (#40# wild-type enzyme Adh 1 <92>) <92>
TN	#43# 230 {4-chloroacetophenone}  (#43# pH 6.0, 37°C, recombinant
	enzyme expressed from Saccharomyces cerevisiae <232>) <232>
TN	#43# 317 {Capronaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
TN	#43# 576 {Capronaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
TN	#43# 303 {phenylacetaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
TN	#43# 418 {Valeraldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
TN	#43# 145 {4-chloroacetophenone}  (#43# pH 6.0, 37°C, recombinant
	enzyme expressed from Hansenula polymorpha <232>) <232>
TN	#43# 264 {phenylacetaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
TN	#43# 410 {Capronaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
TN	#43# 211 {acetophenone}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
TN	#43# 202 {phenylacetaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
TN	#43# 259 {acetophenone}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
TN	#43# 288 {acetophenone}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
TN	#43# 432 {Valeraldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
TN	#43# 432 {4-chloroacetophenone}  (#43# pH 6.0, 37°C, recombinant
	enzyme expressed from Arxula adeninivorans <232>) <232>
TN	#43# 528 {Valeraldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
TN	#45# 3.3 {4-methoxybenzaldehyde}  (#45# wild type enzyme, at 65°C
	<154>) <154>
TN	#45# 3.3 {4-methoxybenzyl alcohol}  (#45# wild type enzyme, at 65°C
	<154>) <154>
TN	#45# 0.5 {ethanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
TN	#45# 1.1 {4-bromobenzyl alcohol}  (#45# native enzyme, at 55°C <153>)
	<153>
TN	#45# 1.1 {4-bromobenzylalcohol}  (#45# in the presence of 3 mM NAD+, in
	0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
TN	#45# 3.5 {benzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5) containing
	0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at 55°C <153>)
	<153,163>
TN	#45# 3.5 {4-bromobenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
TN	#45# 15.9 {Cyclohexanol}  (#45# mutant enzyme N249Y, at 65°C <154>)
	<154>
TN	#45# 1.5 {4-methoxybenzyl alcohol}  (#45# native enzyme, at 55°C
	<153>) <153>
TN	#45# 1.5 {4-methoxybenzylalcohol}  (#45# in the presence of 3 mM NAD+,
	in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
TN	#45# 2.6 {1-propanol}  (#45# wild type enzyme, at 65°C <154>) <154>
TN	#45# 0.7 {4-carboxybenzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5)
	containing 0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at
	55°C <153>) <153,163>
TN	#45# 2 {NADH}  (#45# carboxymethylated enzyme, at 55°C <153>) <153>
TN	#45# 2 {3-bromobenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
TN	#45# 2.2 {1-propanol}  (#45# carboxymethylated enzyme, at 55°C <153>)
	<153>
TN	#45# 3.1 {methanol}  <66>
TN	#45# 1.4 {benzyl alcohol}  (#45# native enzyme, at 55°C <153>) <153>
TN	#45# 1.4 {benzylalcohol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>) <163>
TN	#45# 1.4 {3-Methoxybenzyl alcohol}  (#45# native enzyme, at 55°C
	<153>) <153>
TN	#45# 1.4 {3-methoxybenzylalcohol}  (#45# in the presence of 3 mM NAD+,
	in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
TN	#45# 16 {3-Methoxybenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
TN	#45# 0.65 {Cyclohexanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
TN	#45# 21.7 {benzyl alcohol}  (#45# mutant enzyme N249Y, at 65°C <154>)
	<154>
TN	#45# 0.6 {4-methoxybenzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5)
	containing 0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at
	55°C <153>) <153,163>
TN	#45# 50 {NAD+}  (#45# mutant enzyme N249Y, at 65°C, in the presence of
	benzyl alcohol <154>) <154>
TN	#45# 20.5 {4-methoxybenzaldehyde}  (#45# mutant enzyme N249Y, at 65°C
	<154>) <154>
TN	#45# 20.5 {4-methoxybenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
TN	#45# 0.45 {2-propanol}  (#45# carboxymethylated enzyme, at 55°C <153>)
	<153>
TN	#45# 4.6 {4-Nitrobenzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5)
	containing 0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at
	55°C <153>) <153,163>
TN	#45# 1.2 {1-propanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
TN	#45# 1.2 {3-methoxybenzylalcohol}  (#45# in the presence of 5 mM
	benzylalcohol, in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
TN	#45# 1.2 {3-bromobenzyl alcohol}  (#45# native enzyme, at 55°C <153>)
	<153>
TN	#45# 1.2 {3-bromobenzylalcohol}  (#45# in the presence of 3 mM NAD+, in
	0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
TN	#45# 4.5 {NADH}  (#45# in 50 mM Tris-HCl (pH 7.5) containing 0.25 mM
	benzaldehyde, at 65°C <163>; #45# native enzyme, at 55°C <153>)
	<153,163>
TN	#45# 1.8 {benzaldehyde}  (#45# carboxymethylated enzyme, at 55°C
	<153>) <153>
TN	#45# 2.17 {3-methylcyclohexanone}  <66>
TN	#45# 1.02 {Cyclopentanone}  <66>
TN	#45# 0.25 {2-propanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
TN	#45# 25.5 {benzaldehyde}  (#45# mutant enzyme N249Y, at 65°C <154>)
	<154>
TN	#45# 25.5 {4-methoxybenzyl alcohol}  (#45# mutant enzyme N249Y, at
	65°C <154>) <154>
TN	#45# 0.85 {ethanol}  (#45# carboxymethylated enzyme, at 55°C <153>)
	<153>
TN	#45# 0.317 {acetone}  <66>
TN	#45# 14.5 {benzyl alcohol}  (#45# carboxymethylated enzyme, at 55°C
	<153>) <153>
TN	#45# 7.72 {3-methyl-cyclohexanol}  <66>
TN	#45# 0.983 {Anisaldehyde}  <66>
TN	#45# 1.22 {3-methylbutan-2-one}  <66>
TN	#45# 1.68 {benzyl alcohol}  <66>
TN	#45# 1.88 {ethanol}  <66>
TN	#45# 1.93 {butan-2-one}  <66>
TN	#45# 1.97 {butan-1-ol}  <66>
TN	#45# 2.92 {pentan-3-ol}  <66>
TN	#45# 3.55 {butan-2-ol}  <66>
TN	#45# 3.82 {pentan2-ol}  <66>
TN	#45# 4.03 {propan-1-ol}  <66>
TN	#45# 6.92 {propan-2-ol}  <66>
TN	#45# 16.6 {1-propanol}  (#45# mutant enzyme N249Y, at 65°C <154>) <154>
TN	#45# 25.3 {NADH}  (#45# mutant enzyme N249Y, at 65°C, in the presence
	of benzaldehyde <154>) <154>
TN	#45# 18.5 {NAD+}  (#45# carboxymethylated enzyme, at 55°C <153>) <153>
TN	#45,104# 11.3 {benzaldehyde}  (#45# wild type enzyme, at 65°C <154>;
	#104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at
	65°C <207>) <154,207>
TN	#45,104# 3.6 {benzyl alcohol}  (#45# wild type enzyme, at 65°C <154>;
	#104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at
	65°C <207>) <154,207>
TN	#45,104# 10.3 {NADH}  (#45# wild type enzyme, at 65°C, in the presence
	of benzaldehyde <154>; #104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <154,207>
TN	#45,104# 1.2 {Cyclohexanol}  (#45# carboxymethylated enzyme, at 55°C
	<153>; #45# wild type enzyme, at 65°C <154>; #104# wild type enzyme,
	in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <153,154,207>
TN	#45,104,118# 3.4 {NAD+}  (#45# wild type enzyme, at 65°C, in the
	presence of benzyl alcohol <154>; #104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>; #118# mutant W49F/W167Y,
	30°C, pH not specified in the publication <257>) <154,207,257>
TN	#45,118# 1.4 {NAD+}  (#45# in 0.1 M glycine-NaOH, pH 9.2, at 65°C
	<163>; #45# native enzyme, at 55°C <153>; #118# mutant
	W49F/W167Y/V260A, 30°C, pH not specified in the publication <257>)
	<153,163,257>
TN	#5# 0.45 {Hexanol}  (#5# recombinant isozyme ADH1, pH 7.5, 25°C <119>)
	<119>
TN	#5# 3.83 {Hexanol}  (#5# recombinant isozyme ADH1, pH 10.5, 25°C
	<119>) <119>
TN	#5# 1.92 {ethanol}  (#5# recombinant isozyme ADH1, pH 7.5, 25°C <119>)
	<119>
TN	#5# 4.42 {ethanol}  (#5# recombinant isozyme ADH1, pH 10.5, 25°C
	<119>) <119>
TN	#5# 30.8 {Hexanol}  (#5# recombinant isozyme ADH4, pH 7.5, 25°C <119>)
	<119>
TN	#5# 41.3 {ethanol}  (#5# recombinant isozyme ADH4, pH 7.5, 25°C <119>)
	<119>
TN	#5# 215 {ethanol}  (#5# recombinant isozyme ADH4, pH 10.5, 25°C <119>)
	<119>
TN	#5# 86.5 {Hexanol}  (#5# recombinant isozyme ADH4, pH 10.5, 25°C
	<119>) <119>
TN	#6# 1.1 {(S)-1-phenylethanol}  (#6# pH 10.5, 65°C <169>) <169>
TN	#6# 1.1 {(S)-(-)-1-phenylethanol}  (#6# 65°C <169>) <169>
TN	#6# 1.6 {4-methoxybenzyl alcohol}  (#6# 65°C <169>; #6# pH 10.5, 65°C
	<169>) <169>
TN	#6# 3.1 {4-methoxybenzaldehyde}  (#6# pH 6.0, 65°C <169>) <169>
TN	#6# 3.1 {3-Methoxybenzaldehyde}  (#6# 65°C <169>) <169>
TN	#6# 0.84 {NAD+}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>) <169>
TN	#6# 7.7 {alpha-tetralone}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>)
	<169>
TN	#6# 45.7 {1-Indanol}  (#6# 65°C <169>) <169>
TN	#6# 8.3 {1-Indanone}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>) <169>
TN	#6# 52.4 {NADH}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>) <169>
TN	#6# 57 {(S)-alpha-tetralol}  (#6# pH 10.5, 65°C <169>) <169>
TN	#6# 57 {(S)-(+)-alpha-tetraol}  (#6# 65°C <169>) <169>
TN	#6# 17.1 {1-phenyl-1,2-propanedione}  (#6# 65°C <169>) <169>
TN	#6# 17.1 {1-phenyl-1,2-propandione}  (#6# pH 10.5, 65°C <169>) <169>
TN	#6# 25.5 {2,2,2-trifluoroacetophenone}  (#6# 65°C <169>; #6# pH 10.5,
	65°C <169>) <169>
TN	#6# 38.1 {methylbenzoylformate}  (#6# 65°C <169>) <169>
TN	#6# 38.1 {methyl oxo(phenyl)acetate}  (#6# pH 10.5, 65°C <169>) <169>
TN	#6# 50.1 {ethyl benzoylformate}  (#6# 65°C <169>) <169>
TN	#6# 50.1 {ethyl oxo(phenyl)acetate}  (#6# pH 10.5, 65°C <169>) <169>
TN	#6# 48.1 {alpha-tetralol}  (#6# 65°C <169>) <169>
TN	#6# 61.4 {(S)-1-indanol}  (#6# pH 10.5, 65°C <169>) <169>
TN	#6# 61.4 {(S)-(+)-1-indanol}  (#6# 65°C <169>) <169>
TN	#68# 4.92 {ethanol}  (#68# enzyme form ADH-2 <60>) <60>
TN	#68# 17 {octanal}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 8.88 {NADH}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 0.75 {Cyclohexanol}  (#68# enzyme form ADH-2 <60>) <60>
TN	#68# 7.22 {butan-1-ol}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 1.45 {12-hydroxydodecanoate}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 2.52 {benzyl alcohol}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 1.85 {octan-1-ol}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 4.67 {NAD+}  (#68# enzyme form ADH-2 <60>) <60>
TN	#68# 2.92 {pentan-1-ol}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 3.55 {Cyclohexanol}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 6.18 {NAD+}  (#68# enzyme form ADH-3 <60>) <60>
TN	#68# 6.63 {ethanol}  (#68# enzyme form ADH-3 <60>) <60>
TN	#78# 0.117 {methanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>)
	<24>
TN	#78# 16.7 {acetaldehyde}  (#78# pyrazole-sensitive enzyme, pH 7.0 <24>)
	<24>
TN	#78# 0.45 {ethanol}  (#78# pyrazole-insensitive enzyme, pH 10.0 <24>)
	<24>
TN	#78# 0.45 {butanol}  (#78# pyrazole-sensitive enzyme and
	pyrazole-insensitive enzyme, pH 10.0 <24>) <24>
TN	#78# 3.33 {acetaldehyde}  (#78# pyrazole-insensitive enzyme, pH 7.0
	<24>) <24>
TN	#78# 0.333 {Pentanol}  (#78# pyrazole-sensitive enzyme, pH 10.0 <24>)
	<24>
TN	#78# 0.35 {butanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>) <24>
TN	#78# 0.217 {methanol}  (#78# pyrazole-sensitive enzyme, pH 10.0 <24>)
	<24>
TN	#78# 0.567 {ethanol}  (#78# pyrazole-sensitive enzyme <24>) <24>
TN	#78# 0.0833 {ethanol}  (#78# pyrazole-insensitive enzyme, pH 7.5 <24>)
	<24>
TN	#78# 0.0833 {butanol}  (#78# pyrazole-insensitive enzyme, pH 7.5 <24>)
	<24>
TN	#78# 0.283 {Pentanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>)
	<24>
TN	#8# 0.55 {all-trans-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B2 <107>)
	<107>
TN	#8# 0.4 {all-trans-retinol}  <53>
TN	#8# 8 {Pentanol}  <14>
TN	#8# 0.7 {ethanol}  (#8# pH 7.5, anodic enzyme form <18>) <18>
TN	#8# 0.7 {butanol}  (#8# pH 7.5, anodic enzyme form <18>) <18>
TN	#8# 0.9 {all-trans-retinol}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
TN	#8# 0.04 {Octanol}  (#8# recombinant allozyme Val308, pH 7.5, 25°C
	<115>) <115>
TN	#8# 16 {Pentanol}  <53>
TN	#8# 2.5 {ethanol}  (#8# per active site <12>) <12>
TN	#8# 2.5 {3,4-dihydro-retinol}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
TN	#8# 6.17 {16-hydroxyhexadecanoate}  <14>
TN	#8# 20 {4-oxo-retinal}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>) <107>
TN	#8# 4 {ethanol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
TN	#8# 4 {12-hydroxydodecanoate}  <14>
TN	#8# 0.11 {retinol}  (#8# recombinant allozyme Val308, pH 7.5, 25°C
	<115>) <115>
TN	#8# 3.83 {ethanol}  (#8# isoenzyme gamma1,gamma1 <13>) <13>
TN	#8# 4.33 {Octanol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
TN	#8# 0.167 {ethanol}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C
	<115>) <115>
TN	#8# 0.167 {4-oxo-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B1 <107>)
	<107>
TN	#8# 0.183 {1-Pentanol}  <11>
TN	#8# 0.583 {Cyclohexanol}  <14>
TN	#8# 0.75 {2-propanol}  <14>
TN	#8# 0.75 {ethylene glycol}  <14>
TN	#8# 2.83 {1-Octanol}  <11>
TN	#8# 2.83 {2-deoxy-D-ribose}  <14>
TN	#8# 2.83 {4-hydroxy-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B2 <107>)
	<107>
TN	#8# 7.5 {3-Phenyl-1-propanol}  <14>
TN	#8# 3.33 {octanal}  <16>
TN	#8# 7.33 {Octanol}  <16>
TN	#8# 0.333 {12-Hydroxydodecanoic acid}  <11>
TN	#8# 2.17 {(S)-2-butanol}  <53>
TN	#8# 0.018 {all-trans-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B1
	<107>) <107>
TN	#8# 0.092 {4-hydroxy-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B1
	<107>) <107>
TN	#8# 0.25 {all-trans-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B2 <107>)
	<107>
TN	#8# 0.667 {Pentanol}  (#8# pH 7.5, anodic enzyme form <18>) <18>
TN	#8# 0.038 {Octanol}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C
	<115>) <115>
TN	#8# 2.95 {12-hydroxydodecanoate}  <53>
TN	#8# 8.33 {Octanol}  <14>
TN	#8# 9.17 {benzyl alcohol}  <14>
TN	#8# 0.22 {3,4-dihydro-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B2
	<107>) <107>
TN	#8# 4.67 {benzyl alcohol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
TN	#8# 17.2 {Propanol}  <53>
TN	#8# 0.245 {Pentanol}  <16>
TN	#8# 0.717 {NAD+}  (#8# pH 7.5, anodic enzyme form <18>) <18>
TN	#8# 1.83 {all-trans-retinal}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
TN	#8# 1.83 {tryptophol}  <14>
TN	#8# 0.102 {methanol}  <12>
TN	#8# 0.467 {Vanillyl alcohol}  <16>
TN	#8# 0.683 {3-Pyridylcarbinol}  (#8# pH 7.5, anodic enzyme form <18>)
	<18>
TN	#8# 1.22 {3,4-dihydro-retinal}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
TN	#8# 3.03 {12-hydroxydodecanoate}  <16>
TN	#8# 7.83 {ethanol}  <14>
TN	#8# 7.83 {4-oxo-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B2 <107>)
	<107>
TN	#8# 8.67 {Vanillyl alcohol}  <14>
TN	#8# 10.2 {ethanol}  (#8# pH 10.0, anodic enzyme form <18>) <18>
TN	#8# 19.5 {Hexanol}  <53>
TN	#8# 30.7 {ethanol}  <53>
TN	#8# 34.8 {butanol}  <53>
TN	#8# 0.175 {ethanol}  (#8# recombinant allozyme Val308, pH 7.5, 25°C
	<115>) <115>
TN	#8# 0.028 {all-trans-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B1
	<107>) <107>
TN	#8# 0.087 {retinol}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C
	<115>) <115>
TN	#8# 34.2 {4-hydroxy-retinol}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
TN	#8# 0.088 {3,4-dihydro-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B2
	<107>) <107>
TN	#82# 1.1 {butanol}  <101>
TN	#82# 0.05 {methanol}  <101>
TN	#82# 0.15 {Octanol}  <101>
TN	#82# 0.167 {Cyclohexanol}  <101>
TN	#82# 0.167 {Hexanol}  <101>
TN	#82# 0.467 {ethanol}  <101>
TN	#84# 3.97 {ethyl pyruvate}  (#84# pH 6.5, 50°C, recombinant enzyme
	<226>) <226>
TN	#9# 0.833 {1-butanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 1 {ethanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 1 {benzyl alcohol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 1 {1-Octanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 1.5 {Cyclohexanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 1.17 {1-Pentanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 20 {12-hydroxydodecanoate}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9# 1.67 {2-Buten-1-ol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
TN	#9# 3.83 {12-hydroxydodecanoate}  (#9# isoenzyme ADH-12, pH 10.0 <49>)
	<49>
TN	#9# 1.27 {12-hydroxydodecanoate}  (#9# isoenzyme ADH-3, pH 10.0 <49>)
	<49>
TN	#9# 5.83 {2-Buten-1-ol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
TN	#9# 2.33 {1-Octanol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
TN	#9# 0.383 {Cyclohexanol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
TN	#9# 213 {2-Buten-1-ol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9# 3.53 {1-Pentanol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
TN	#9# 48.8 {1-butanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9# 48.8 {1-Pentanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9# 60.8 {1-Octanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9# 62.7 {ethanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9# 89.7 {benzyl alcohol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
TN	#9,35# 1.75 {Cyclohexanol}  (#35# isoenzyme BB-ADH <95>; #9# isoenzyme
	ADH-1, pH 10.0 <49>) <49,95>
TN	#91# 39.9 {ethanol}  (#91# 10°C, pH 9.0 <144>) <144>
TN	#91# 62.48 {ethanol}  (#91# 20°C, pH 9.0 <144>) <144>
TN	#91# 109.5 {ethanol}  (#91# 30°C, pH 9.0 <144>) <144>
TN	#91# 160.8 {ethanol}  (#91# 40°C, pH 9.0 <144>) <144>
TN	#91# 262.3 {ethanol}  (#91# 50°C, pH 9.0 <144>) <144>
TN	#91# 474.9 {ethanol}  (#91# 60°C, pH 9.0 <144>) <144>
TN	#98# 0.00086 {ethanol}  <173>

KM_VALUE
KM	#10# 0.22 {acetaldehyde}  (#10# wild-type, pH 6.7, 30°C <282>) <282>
KM	#10# 0.13 {furfural}  (#10# mutant S110P/Y295C, pH 6.7, 30°C <282>)
	<282>
KM	#10# 11 {p-methoxybenzyl alcohol}  (#10# isozyme ADH1, in the presence
	of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA
	buffer, pH 7.3, at 30°C <202>) <202>
KM	#10# 0.059 {NAD+}  <87>
KM	#10# 0.83 {acetaldehyde}  (#10# mutant S110P/Y295C, pH 6.7, 30°C
	<282>) <282>
KM	#10# 14 {ethanol}  (#10# in presence of 3 mM SDS <192>) <192>
KM	#10# 14 {benzaldehyde}  (#10# isozyme ADH2, in the presence of 0.25 mM
	NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer,
	pH 7.3, at 30°C <202>) <202>
KM	#10# 50 {ethanol}  (#10# in presence of 50 mM SDS <192>) <192>
KM	#10# 2.9 {p-Methoxybenzaldehyde}  (#10# isozyme ADH1, in the presence
	of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM
	EDTA buffer, pH 7.3, at 30°C <202>) <202>
KM	#10# 33 {benzaldehyde}  (#10# isozyme ADH1, in the presence of 0.25 mM
	NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer,
	pH 7.3, at 30°C <202>) <202>
KM	#10# 34 {benzyl alcohol}  (#10# isozyme ADH1, in the presence of 2 mM
	NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer,
	pH 7.3, at 30°C <202>) <202>
KM	#10# 12.1 {ethanol}  (#10# 40°C, pH 9.0 <144>) <144>
KM	#10# 37 {formaldehyde}  (#10# pH 7.0, 30°C <285>) <285>
KM	#10# 42 {furfural}  (#10# pH 7.0, 30°C <285>) <285>
KM	#10# 49 {benzyl alcohol}  (#10# isozyme ADH2, in the presence of 2 mM
	NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer,
	pH 7.3, at 30°C <202>) <202>
KM	#10# 53 {ethanol}  (#10# pH 7.5, 25°C, native Zn-ADH <122>) <122>
KM	#10# 350 {beta-NAD+}  (#10# in presence of 1 mM SDS <192>) <192>
KM	#10# 0.122 {NADH}  <87>
KM	#10# 5.9 {p-Methoxybenzaldehyde}  (#10# isozyme ADH2, in the presence
	of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM
	EDTA buffer, pH 7.3, at 30°C <202>) <202>
KM	#10# 18.8 {furfural}  (#10# wild-type, pH 6.7, 30°C <282>) <282>
KM	#10# 39 {ethanol}  (#10# pH 7.5, 25°C, Cu-ADH <122>) <122>
KM	#10# 16.7 {ethanol}  <87>
KM	#10# 41 {ethanol}  (#10# in presence of 15 mM SDS <192>) <192>
KM	#10# 41 {propanal}  (#10# pH 7.0, 30°C <285>) <285>
KM	#10# 240 {beta-NAD+}  (#10# in presence of 0.5 mM SDS <192>) <192>
KM	#10# 6.9 {p-methoxybenzyl alcohol}  (#10# isozyme ADH2, in the presence
	of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA
	buffer, pH 7.3, at 30°C <202>) <202>
KM	#10# 2.83 {acetaldehyde}  <87>
KM	#10# 72 {Butanal}  (#10# pH 7.0, 30°C <285>) <285>
KM	#10# 88 {glycolaldehyde}  (#10# pH 7.0, 30°C <285>) <285>
KM	#10# 710 {beta-NAD+}  (#10# in presence of 3 mM SDS <192>) <192>
KM	#10# 8.56 {ethanol}  (#10# 30°C, pH 9.0 <144>) <144>
KM	#10# 9.45 {5-hydroxymethylfurfural}  (#10# mutant S110P/Y295C, pH 6.7,
	30°C <282>) <282>
KM	#10# 7.75 {ethanol}  (#10# in 50 mM Tris-HCl, pH 8.0 at 25°C <209>)
	<209>
KM	#10# 9.03 {ethanol}  (#10# 10°C, pH 9.0 <144>) <144>
KM	#10# 243 {beta-NAD+}  (#10# in presence of 0.5 mM SDS <192>) <192>
KM	#10# 2290 {beta-NAD+}  (#10# in presence of 15 mM SDS <192>) <192>
KM	#10# 1230 {beta-NAD+}  (#10# in presence of 50 mM SDS <192>) <192>
KM	#10# 24.45 {phenylglyoxylic acid}  (#10# soluble enzyme <182>) <182>
KM	#10# 37.55 {phenylglyoxylic acid}  (#10# enzyme covalently immobilized
	to magnetic Fe3O4 nanoparticles via glutaraldehyde <182>) <182>
KM	#10,110# 5.7 {ethanol}  (#10# 20°C, pH 9.0 <144>; #110# in 100 mM
	Tris-HCl, at pH 5.0 and 75°C <213>) <144,213>
KM	#10,138# 17 {ethanol}  (#10# in presence of 1 mM SDS <192>; #138# pH
	7.0, temperature not specified in the publication <252>) <192,252>
KM	#10,66,80# 12 {ethanol}  (#10# pH 7.5, 25°C, Co-ADH <122>) <77,78,122>
KM	#10,89# 13 {ethanol}  (#89# pH 8.5 <105>; #10# in presence of 0.5 mM
	SDS <192>) <105,192>
KM	#100# 0.87 {NADH}  (#100# pH 6.0 <185>) <185>
KM	#100# 0.13 {N-benzyl-3-pyrrolidinone}  (#100# pH 6.0 <185>) <185>
KM	#100# 0.79 {NAD+}  (#100# pH 8.0 <185>) <185>
KM	#100# 8.47 {(S)-N-benzyl-3-pyrrolidinol}  (#100# pH 8.0 <185>) <185>
KM	#104# 66 {ethanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.26 {1-Pentanol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.26 {Isobutyraldehyde}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.41 {(R)-2-butanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.012 {(S)-2-butanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.008 {NADH}  (#104# mutant enzyme W95L, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.04 {1-Hexanol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.21 {1-Heptanol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.027 {1-Pentanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.038 {1-Heptanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.09 {trans-cinnamaldehyde}  (#104# mutant enzyme W95L,, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.07 {benzaldehyde}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.07 {Butyraldehyde}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.07 {4-methoxybenzyl alcohol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.07 {(S)-2-pentanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.009 {trans-cinnamaldehyde}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.12 {benzyl alcohol}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.12 {4-methoxybenzyl alcohol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.25 {2-ethoxyethanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.28 {benzaldehyde}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 4.6 {ethanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.22 {(R)-2-pentanol}  (#104# wild type enzyme, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.67 {1-Heptanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.23 {trans-cinnamaldehyde}  (#104# mutant enzyme W95L/N249Y, in
	0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 1.9 {1-Pentanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.08 {1-butanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.33 {Isobutyraldehyde}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 4 {NAD+}  (#104# mutant enzyme W95L, in 0.1 M glycine-NaOH buffer
	(pH 10.5), at 65°C <207>) <207>
KM	#104# 0.13 {Butyraldehyde}  (#104# mutant enzyme W95L, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.035 {1-Hexanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 4.5 {Cyclohexanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.27 {Butyraldehyde}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.27 {3-Pentanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 1.6 {1-butanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.75 {NADH}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 50 {NAD+}  (#104# Km above 50 mM, mutant enzyme W95L/N249Y, in
	0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 8.8 {(S)-2-pentanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.24 {1-propanol}  (#104# wild type enzyme, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.76 {Isobutyraldehyde}  (#104# mutant enzyme W95L/N249Y, in 0.1
	M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 29.8 {(S)-2-butanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 3.8 {benzyl alcohol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 0.88 {1-Hexanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 6.5 {1-propanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 11.7 {(R)-2-pentanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104# 37.4 {(R)-2-butanol}  (#104# mutant enzyme W95L/N249Y, in 0.1 M
	glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
KM	#104,111# 0.01 {NADH}  (#111# in 200 mM bicine, pH 6.0, at 60°C <197>;
	#104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at
	65°C <207>) <197,207>
KM	#105# 0.00024 {1-formyl-8-methylpyrene}  (#105# isozyme ADH2, at
	21-23°C <214>) <214>
KM	#105# 0.0005 {1-formylpyrene}  (#105# isozyme ADH1C, at 21-23°C <214>)
	<214>
KM	#105# 0.0009 {1-formyl-6-methylpyrene}  (#105# isozyme ADH1C, at
	21-23°C <214>) <214>
KM	#105# 0.001 {4-formylpyrene}  (#105# isozyme ADH1C, at 21-23°C <214>)
	<214>
KM	#105# 0.001 {4-hydroxymethylpyrene}  (#105# isozyme ADH1C, at 21-23°C
	<214>) <214>
KM	#105# 0.012 {1-formylpyrene}  (#105# isozyme ADH2, at 21-23°C <214>)
	<214>
KM	#105# 0.04 {4-hydroxymethylpyrene}  (#105# isozyme ADH2, at 21-23°C
	<214>) <214>
KM	#105# 0.009 {2-formylpyrene}  (#105# isozyme ADH3, at 21-23°C <214>)
	<214>
KM	#105# 0.00055 {1-formylpyrene}  (#105# isozyme ADH3, at 21-23°C <214>)
	<214>
KM	#105# 0.0021 {2-formylpyrene}  (#105# isozyme ADH1C, at 21-23°C <214>)
	<214>
KM	#105# 0.0021 {4-formylpyrene}  (#105# isozyme ADH3, at 21-23°C <214>)
	<214>
KM	#105# 0.00031 {1-hydroxymethyl-8-methylpyrene}  (#105# isozyme ADH3, at
	21-23°C <214>) <214>
KM	#105# 0.39 {1-Octanol}  (#105# isozyme ADH3, at 21-23°C <214>) <214>
KM	#105# 0.076 {1-hydroxymethylpyrene}  (#105# isozyme ADH2, at 21-23°C
	<214>) <214>
KM	#105# 0.77 {ethanol}  (#105# isozyme ADH1C, at 21-23°C <214>) <214>
KM	#105# 0.00057 {1-hydroxymethyl-6-methylpyrene}  (#105# isozyme ADH3, at
	21-23°C <214>) <214>
KM	#105# 0.34 {acetaldehyde}  (#105# isozyme ADH1C, at 21-23°C <214>)
	<214>
KM	#105# 0.0029 {2-formylpyrene}  (#105# isozyme ADH2, at 21-23°C <214>)
	<214>
KM	#105# 0.059 {1-hydroxymethyl-8-methylpyrene}  (#105# isozyme ADH1C, at
	21-23°C <214>) <214>
KM	#105# 26 {acetaldehyde}  (#105# isozyme ADH2, at 21-23°C <214>) <214>
KM	#105# 0.0044 {2-hydroxymethylpyrene}  (#105# isozyme ADH2, at 21-23°C
	<214>) <214>
KM	#105# 33 {ethanol}  (#105# isozyme ADH2, at 21-23°C <214>) <214>
KM	#105# 0.0064 {1-hydroxymethyl-6-methylpyrene}  (#105# isozyme ADH2, at
	21-23°C <214>) <214>
KM	#105# 0.0064 {1-hydroxymethyl-8-methylpyrene}  (#105# isozyme ADH2, at
	21-23°C <214>) <214>
KM	#105# 0.0038 {4-formylpyrene}  (#105# isozyme ADH2, at 21-23°C <214>)
	<214>
KM	#105# 0.0038 {1-formyl-6-methylpyrene}  (#105# isozyme ADH3, at
	21-23°C <214>) <214>
KM	#105# 9.6 {octanal}  (#105# isozyme ADH3, at 21-23°C <214>) <214>
KM	#105# 0.106 {2-hydroxymethylpyrene}  (#105# isozyme ADH3, at 21-23°C
	<214>) <214>
KM	#105# 0.00059 {1-hydroxymethylpyrene}  (#105# isozyme ADH3, at 21-23°C
	<214>) <214>
KM	#105# 0.00032 {1-formyl-6-methylpyrene}  (#105# isozyme ADH2, at
	21-23°C <214>) <214>
KM	#105# 0.00075 {1-hydroxymethylpyrene}  (#105# isozyme ADH1C, at
	21-23°C <214>) <214>
KM	#105# 0.00131 {1-formyl-8-methylpyrene}  (#105# isozyme ADH1C, at
	21-23°C <214>) <214>
KM	#105# 0.00048 {2-hydroxymethylpyrene}  (#105# isozyme ADH1C, at
	21-23°C <214>) <214>
KM	#105# 0.00037 {4-hydroxymethylpyrene}  (#105# isozyme ADH3, at 21-23°C
	<214>) <214>
KM	#105# 0.00115 {1-hydroxymethyl-6-methylpyrene}  (#105# isozyme ADH1C,
	at 21-23°C <214>) <214>
KM	#105# 0.00149 {1-formyl-8-methylpyrene}  (#105# isozyme ADH3, at
	21-23°C <214>) <214>
KM	#108# 0.00028 {1-hydroxymethyl-6-methylpyrene}  (#108# isozyme ADH4, at
	21-23°C <214>) <214>
KM	#108# 0.033 {2-hydroxymethylpyrene}  (#108# isozyme ADH4, at 21-23°C
	<214>) <214>
KM	#108# 0.0016 {1-hydroxymethyl-8-methylpyrene}  (#108# isozyme ADH4, at
	21-23°C <214>) <214>
KM	#108# 0.00092 {1-formylpyrene}  (#108# isozyme ADH4, at 21-23°C <214>)
	<214>
KM	#108# 0.0029 {4-hydroxymethylpyrene}  (#108# isozyme ADH4, at 21-23°C
	<214>) <214>
KM	#108# 0.0069 {2-formylpyrene}  (#108# isozyme ADH4, at 21-23°C <214>)
	<214>
KM	#108# 3.6 {ethanol}  (#108# isozyme ADH4, at 21-23°C <214>) <214>
KM	#108# 0.000035 {1-formyl-8-methylpyrene}  (#108# isozyme ADH4, at
	21-23°C <214>) <214>
KM	#108# 12.7 {acetaldehyde}  (#108# isozyme ADH4, at 21-23°C <214>) <214>
KM	#108# 0.0283 {1-hydroxymethylpyrene}  (#108# isozyme ADH4, at 21-23°C
	<214>) <214>
KM	#108# 0.00048 {4-formylpyrene}  (#108# isozyme ADH4, at 21-23°C <214>)
	<214>
KM	#108# 0.000036 {1-formyl-6-methylpyrene}  (#108# isozyme ADH4, at
	21-23°C <214>) <214>
KM	#111# 0.13 {NAD+}  (#111# in 200 mM bicine, pH 9.0, at 60°C <197>)
	<197>
KM	#111# 2.09 {Cyclohexanol}  (#111# in 200 mM bicine, pH 9.0, at 60°C
	<197>) <197>
KM	#111# 3.68 {cyclohexanone}  (#111# in 200 mM bicine, pH 6.0, at 60°C
	<197>) <197>
KM	#112# 24 {benzyl alcohol}  (#112# in the presence of 2 mM NAD+, in 83
	mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at
	30°C <202>) <202>
KM	#112# 2-3 {benzaldehyde}  (#112# in the presence of 0.25 mM NADH, in 83
	mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at
	30°C <202>) <202>
KM	#112# 3.4 {p-Methoxybenzaldehyde}  (#112# in the presence of 0.1 mM
	NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer,
	pH 7.3, at 30°C <202>) <202>
KM	#112# 22 {p-methoxybenzyl alcohol}  (#112# in the presence of 2 mM
	NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer,
	pH 7.3, at 30°C <202>) <202>
KM	#113# 0.28 {NADP+}  (#113# cosubstrate ethanol, pH 8.0, 60°C <215>)
	<215>
KM	#113# 1.4 {NADH}  (#113# cosubstrate acetaldehyde, pH 8.0, 60°C <215>)
	<215>
KM	#113# 4.71 {acetaldehyde}  (#113# cosubstrate NADH, pH 8.0, 60°C
	<215>) <215>
KM	#113# 1.51 {NAD+}  (#113# cosubstrate ethanol, pH 8.0, 60°C <215>)
	<215>
KM	#113# 7.55 {ethanol}  (#113# cosubstrate NAD+, pH 8.0, 60°C <215>)
	<215>
KM	#114# 2.4 {NADP+}  (#114# cosubstrate 1-octanol, pH 8.0, 60°C <215>)
	<215>
KM	#114# 1.15 {octanal}  (#114# cosubstrate NADPH, pH 8.0, 60°C <215>)
	<215>
KM	#114# 0.84 {NADPH}  (#114# cosubstrate octanal, pH 8.0, 60°C <215>)
	<215>
KM	#114# 2.25 {acetaldehyde}  (#114# cosubstrate NADPH, pH 8.0, 60°C
	<215>) <215>
KM	#114# 37.6 {ethanol}  (#114# cosubstrate NADP+, pH 8.0, 60°C <215>)
	<215>
KM	#114# 3.88 {1-Octanol}  (#114# cosubstrate NADP+, pH 8.0, 60°C <215>)
	<215>
KM	#114# 1.44 {NAD+}  (#114# cosubstrate 1-octanol, pH 8.0, 60°C <215>)
	<215>
KM	#118# 0.1 {12-hydroxylauric acid methyl ester}  (#118# mutant C257L, pH
	8.0, 60°C <246>) <246>
KM	#118# 1.3 {NAD+}  (#118# mutant W49F/W87F, 30°C, pH not specified in
	the publication <257>) <257>
KM	#118# 1 {NAD+}  (#118# mutant Y25A, 30°C, pH not specified in the
	publication <257>; #118# mutant Y25A, pH 7.0, 30°C <260>) <257,260>
KM	#118# 0.364 {acetaldehyde}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KM	#118# 3.1 {benzyl alcohol}  (#118# mutant W49F/W167Y, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 1.8 {NAD+}  (#118# mutant W49F/W167Y, 30°C, pH not specified in
	the publication <257>) <257>
KM	#118# 10 {NAD+}  (#118# mutant V260A, 30°C, pH not specified in the
	publication <257>) <257>
KM	#118# 0.086 {12-hydroxylauric acid methyl ester}  (#118# wild-type, pH
	8.0, 60°C <246>) <246>
KM	#118# 0.066 {12-oxolauric acid methyl ester}  (#118# wild-type, pH 8.0,
	60°C <246>) <246>
KM	#118# 6.8 {benzyl alcohol}  (#118# wild-type, 30°C, pH not specified
	in the publication <257>) <257>
KM	#118# 8.3 {NAD+}  (#118# mutant W49F/W167Y/V260A, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 1.1 {NAD+}  (#118# wild-type, pH 7.0, 30°C <260>; #118#
	wild-type, 30°C, pH not specified in the publication <257>) <257,260>
KM	#118# 5.4 {benzyl alcohol}  (#118# mutant Y25A/W49F/W167Y/V260A, 30°C,
	pH not specified in the publication <257>) <257>
KM	#118# 4.2 {benzyl alcohol}  (#118# mutant V260A, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 0.108 {Butyraldehyde}  (#118# wild-type, pH 8.0, 60°C <246>)
	<246>
KM	#118# 0.91 {ethanol}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KM	#118# 6 {benzyl alcohol}  (#118# mutant W49F/W87F, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 8.2 {benzyl alcohol}  (#118# mutant W49F/W167Y/V260A, 30°C, pH
	not specified in the publication <257>) <257>
KM	#118# 0.072 {NADH}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KM	#118# 7.2 {benzyl alcohol}  (#118# mutant Y25A, pH 7.0, 30°C <260>)
	<260>
KM	#118# 10.2 {NAD+}  (#118# mutant W49F/W87F/V260A, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 10.9 {benzyl alcohol}  (#118# mutant Y25A/W49F/W87F, 30°C, pH
	not specified in the publication <257>) <257>
KM	#118# 9.7 {NAD+}  (#118# mutant Y25A/W49F/W167Y/V260A, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 0.239 {NAD+}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KM	#118# 10.1 {benzyl alcohol}  (#118# mutant Y25A/W49F/W87F/V260A, 30°C,
	pH not specified in the publication <257>) <257>
KM	#118# 14.8 {NAD+}  (#118# mutant Y25A/W49F/W87F/V260A, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 6.9 {benzyl alcohol}  (#118# wild-type, pH 7.0, 30°C <260>) <260>
KM	#118# 16.5 {benzyl alcohol}  (#118# mutant Y25A, 30°C, pH not
	specified in the publication <257>) <257>
KM	#118# 12.9 {benzyl alcohol}  (#118# mutant W49F/W87F/V260A, 30°C, pH
	not specified in the publication <257>) <257>
KM	#118# 0.611 {n-butanol}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KM	#12# 3.33 {ethanol}  (#12# pH 7.5 <45>) <45>
KM	#12# 0.00694 {NAD+}  (#12# pH 7.5 <45>) <45>
KM	#12# 0.0531 {NAD+}  (#12# pH 10.8 <45>) <45>
KM	#122# 66 {3-methylcyclohexanone}  (#122# 65°C, pH 5.5 <219>) <219>
KM	#122# 1.3 {(R)-alpha-tetralol}  (#122# 65°C, pH 8.0 <219>) <219>
KM	#122# 5.3 {ethyl benzoylformate}  (#122# 65°C, pH 5.5 <219>) <219>
KM	#122# 4.2 {cis-decahydro-1-naphthol}  (#122# 65°C, pH 8.0 <219>) <219>
KM	#122# 12.1 {1-phenyl-1,2-propanedione}  (#122# 65°C, pH 5.5 <219>)
	<219>
KM	#122# 6.5 {methyl benzoylformate}  (#122# 65°C, pH 5.5 <219>) <219>
KM	#122# 9.9 {3-Methylcyclohexanol}  (#122# 65°C, pH 8.0 <219>) <219>
KM	#122# 23.5 {2,2,2-trifluoroacetophenone}  (#122# 65°C, pH 5.5 <219>)
	<219>
KM	#122,123# 0.16 {NADH}  (#123# pH 5.5, 65°C <219>; #122# 65°C, pH 5.5
	<219>) <219>
KM	#122,123# 2.4 {(R)-1-indanol}  (#123# pH 8.0, 65°C <219>; #122# 65°C,
	pH 8.0 <219>) <219>
KM	#122,123# 0.71 {isatin}  (#123# pH 5.5, 65°C <219>; #122# 65°C, pH
	5.5 <219>) <219>
KM	#122,123# 2.8 {methyl o-chlorobenzoylformate}  (#123# pH 5.5, 65°C
	<219>; #122# 65°C, pH 5.5 <219>) <219>
KM	#122,123# 1.05 {(S)-alpha-tetralol}  (#123# pH 8.0, 65°C <219>; #122#
	65°C, pH 8.0 <219>) <219>
KM	#122,123# 6.4 {(S)-1-indanol}  (#123# pH 8.0, 65°C <219>; #122# 65°C,
	pH 8.0 <219>) <219>
KM	#122,123# 0.44 {NAD+}  (#123# pH 8.0, 65°C <219>; #122# 65°C, pH 8.0
	<219>) <219>
KM	#122,123# 9.3 {cycloheptanol}  (#123# pH 8.0, 65°C <219>; #122# 65°C,
	pH 8.0 <219>) <219>
KM	#123# 0.11 {2,2-dichloroacetophenone}  (#123# 65°C, pH 5.0 <218>) <218>
KM	#123# 0.43 {benzil}  (#123# 65°C, pH 5.0 <218>) <218>
KM	#123# 0.81 {isoborneol}  (#123# 65°C, pH 10.5 <218>) <218>
KM	#123# 4.2 {ethyl benzoylformate}  (#123# 65°C, pH 5.0 <218>) <218>
KM	#123# 5 {1-phenyl-1,2-propanedione}  (#123# 65°C, pH 5.0 <218>) <218>
KM	#123# 5.1 {cycloheptanol}  (#123# 65°C, pH 10.5 <218>) <218>
KM	#123# 11.9 {2',3',4',5',6'-pentafluoroacetophenone}  (#123# 65°C, pH
	5.0 <218>) <218>
KM	#123# 6.3 {2,2,2-trifluoroacetophenone}  (#123# 65°C, pH 5.0 <218>)
	<218>
KM	#123# 8.5 {tetralin-1-ol}  (#123# 65°C, pH 10.5 <218>) <218>
KM	#123# 8.7 {1-Indanol}  (#123# 65°C, pH 10.5 <218>) <218>
KM	#123# 1.28 {(R)-alpha-tetralol}  (#123# pH 8.0, 65°C <219>) <219>
KM	#123# 16.6 {ethyl 3-methyl-2-oxobutyrate}  (#123# 65°C, pH 5.0 <218>)
	<218>
KM	#126# 0.67 {acetaldehyde}  (#126# pH 6.0, 22°C, recombinant enzyme
	<222>) <222>
KM	#13# 0.03 {cinnamaldehyde}  (#13# pH 7.7, 60°C <234>) <234>
KM	#13# 0.11 {cinnamyl alcohol}  (#13# pH 7.7, 60°C <234>) <234>
KM	#13# 0.45 {NAD+}  (#13# pH 7.7, 60°C <234>) <234>
KM	#13# 0.016 {NADH}  (#13# pH 7.7, 60°C <234>) <234>
KM	#13# 57.8 {2-propanol}  (#13# pH 7.7, 60°C <234>) <234>
KM	#13# 5.11 {ethanol}  <126>
KM	#130# 0.6 {Octanol}  (#130# pH and temperature not specified in the
	publication <227>) <227>
KM	#131# 0.147 {1-Hexanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.147 {2-decanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.001 {NAD+}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.0004 {NADH}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.396 {1-Pentanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 1.05 {2-butanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.286 {2-Octanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.333 {benzaldehyde}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 1.13 {4-methoxybenzyl alcohol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.131 {4-methoxyphenylacetone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 1.03 {1-propanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 1.16 {2-Heptanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 1.39 {cyclohexanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.215 {2-nonanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.752 {2-Pentanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 5.15 {2-Pentanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.703 {Cyclohexanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 13.7 {ethanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 2.44 {2-propanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 5.43 {benzyl alcohol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.694 {tert-butyl acetoacetate}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 0.596 {1-butanol}  (#131# pH 8.0, 60°C <239>) <239>
KM	#131# 5.01 {2-Hexanone}  (#131# pH 8.0, 60°C <239>) <239>
KM	#132# 0.29 {NAD+}  (#132# pH 11.0, temperature not specified in the
	publication <237>) <237>
KM	#132# 31 {ethanol}  (#132# pH 11.0, temperature not specified in the
	publication <237>) <237>
KM	#132# 28 {acetaldehyde}  (#132# pH 6.0, temperature not specified in
	the publication <237>) <237>
KM	#135# 4 {acetaldehyde}  (#135# pH 7.0, temperature not specified in the
	publication <252>) <252>
KM	#135# 39.7 {ethanol}  (#135# pH 7.0, temperature not specified in the
	publication <252>) <252>
KM	#136# 1.2 {acetaldehyde}  (#136# pH 7.0, temperature not specified in
	the publication <252>) <252>
KM	#136# 49.5 {ethanol}  (#136# pH 7.0, temperature not specified in the
	publication <252>) <252>
KM	#137# 26 {ethanol}  (#137# pH 7.0, temperature not specified in the
	publication <252>) <252>
KM	#14# 1.3 {ethanol}  <81>
KM	#14# 1.3 {propan-2-ol}  <81>
KM	#14# 0.35 {NADH}  <81>
KM	#14# 0.053 {acetaldehyde}  <81>
KM	#14# 550 {NAD+}  (#14# reduction of propan-2-ol <81>) <81>
KM	#14,118# 0.9 {NAD+}  (#14# reduction of ethanol <81>; #118# mutant
	Y25A/W49F/W87F, 30°C, pH not specified in the publication <257>)
	<81,257>
KM	#141# 16 {benzyl alcohol}  (#141# mutant A25Y, pH 7.0, 30°C <260>)
	<260>
KM	#141# 29.4 {benzyl alcohol}  (#141# wild-type, pH 7.0, 30°C <260>)
	<260>
KM	#142# 0.6 {NAD+}  (#142# pH 8.8, 70°C <138>) <138>
KM	#142# 0.097 {NADH}  (#142# pH 6.1, 70°C <138>) <138>
KM	#142# 6.5 {acetoin}  (#142# reduction reaction, pH 6.1, 70°C <138>)
	<138>
KM	#142# 86.8 {Butan-2,3-diol}  (#142# pH 8.8, 70°C <138>) <138>
KM	#148# 0.062 {NADH}  (#148# alcohol dehydrogenase domain, 60°C, pH 6.0,
	presence of 0.1 mM Zn2+ <241>) <241>
KM	#148# 0.038 {NADH}  (#148# wild-type, 60°C, pH 6.0, presence of 0.1 mM
	Zn2+ <241>) <241>
KM	#148# 34 {acetaldehyde}  (#148# wild-type, 60°C, pH 6.0, presence of
	0.1 mM Zn2+ <241>) <241>
KM	#148# 121 {acetaldehyde}  (#148# alcohol dehydrogenase domain, 60°C,
	pH 6.0, presence of 0.1 mM Zn2+ <241>) <241>
KM	#149# 0.089 {NAD+}  (#149# cosubstrate 1-phenylethanol, pH 9.0, 70°C
	<243>) <243>
KM	#149# 0.066 {NADP+}  (#149# cosubstrate 1-phenylethanol, pH 9.0, 70°C
	<243>) <243>
KM	#149# 0.113 {NADH}  (#149# cosubstrate acetoin, pH 6.0, 70°C <243>)
	<243>
KM	#149# 0.113 {NADP+}  (#149# cosubstrate 2,3-butanediol, pH 9.0, 70°C
	<243>) <243>
KM	#149# 0.127 {NAD+}  (#149# cosubstrate 2,3-butanediol, pH 9.0, 70°C
	<243>) <243>
KM	#149# 244 {1-phenylethanol}  (#149# pH 9.0, 70°C <243>) <243>
KM	#149# 30.2 {acetoin}  (#149# pH 6.0, 70°C <243>) <243>
KM	#149# 61.3 {2,3-Butanediol}  (#149# pH 9.0, 70°C <243>) <243>
KM	#150# 0.6 {NADPH}  (#150# pH 6.5, 65°C <244>) <244>
KM	#150# 0.4 {benzaldehyde}  (#150# pH 6.5, 65°C <244>) <244>
KM	#150# 3.3 {(2E)-but-2-enal}  (#150# pH 6.5, 65°C <244>) <244>
KM	#150# 0.7 {NADP+}  (#150# pH 8.0, 55°C <244>) <244>
KM	#150# 14 {benzyl alcohol}  (#150# pH 8.0, 55°C <244>) <244>
KM	#150# 9.1 {(2E)-but-2-en-1-ol}  (#150# pH 8.0, 55°C <244>) <244>
KM	#154# 0.02 {NAD+}  (#154# cosubstrate butan-1-ol, pH 7.0, 30°C <271>)
	<271>
KM	#154# 0.09 {NADH}  (#154# cosubstrate butanal, pH 7.0, 30°C <271>)
	<271>
KM	#154# 0.48 {Butanal}  (#154# cosubstrate NADH, pH 7.0, 30°C <271>)
	<271>
KM	#154# 5.65 {butan-1-ol}  (#154# cosubstrate NAD+, pH 7.0, 30°C <271>)
	<271>
KM	#16# 3.5 {ethanol}  (#16# isoenzyme III from leaf <79>) <79>
KM	#16# 25 {NADH}  (#16# isoenzyme III from leaf <79>) <79>
KM	#16# 70 {NADH}  (#16# isoenzyme II from leaf <79>) <79>
KM	#16# 30 {NAD+}  (#16# isoenzyme II from leaf <79>) <79>
KM	#16# 31 {NAD+}  (#16# isoenzyme III from leaf <79>) <79>
KM	#16# 73 {NAD+}  (#16# isoenzyme I from leaf <79>) <79>
KM	#16# 7.2 {ethanol}  (#16# isoenzyme II from leaf <79>) <79>
KM	#16# 1.45 {acetaldehyde}  (#16# isoenzyme I <79>) <79>
KM	#16# 27.5 {ethanol}  (#16# isoenzyme I from leaf <79>) <79>
KM	#16# 121 {NADH}  (#16# isoenzyme I from leaf <79>) <79>
KM	#16,67# 1.25 {acetaldehyde}  (#16# isoenzyme II <79>) <69,79>
KM	#18# 0.038 {NAD+}  (#18# mutant enzyme ADH1-1S1108 <97>) <97>
KM	#18# 24 {ethanol}  (#18# wild-type enzyme ADH1-1S <97>) <97>
KM	#18# 0.042 {NADH}  (#18# mutant enzyme ADH1-1S1108 <97>) <97>
KM	#18# 0.085 {NADH}  (#18# wild-type enzyme ADH1-1S <97>) <97>
KM	#18# 0.037 {NAD+}  (#18# wild-type enzyme ADH1-1S <97>) <97>
KM	#18# 70 {acetaldehyde}  (#18# mutant enzyme ADH1-1S1108 <97>) <97>
KM	#18# 85 {acetaldehyde}  (#18# wild-type enzyme ADH1-1S <97>) <97>
KM	#18,40# 22 {ethanol}  (#40# pH 7.6 <28>; #18# mutant enzyme ADH1S-1108
	<97>) <28,97>
KM	#19,40# 16 {ethanol}  (#40# pH 8.8 <28>) <28,71>
KM	#20# 5.1 {ethanol}  (#20# pH 10.5, 25°C <284>) <284>
KM	#20# 1.65 {NAD+}  (#20# pH 10.5, 25°C <284>) <284>
KM	#21# 0.6 {acetaldehyde}  <72>
KM	#21# 35 {methylglyoxal}  <72>
KM	#25# 0.58 {N-benzyl-3-pyrrolidinone}  <188>
KM	#26# 200 {ethylene glycol}  (#26# above <129>) <129>
KM	#26# 1.64 {ethanol}  <135>
KM	#27# 20 {ethanol}  (#27# 23°C <74>) <74>
KM	#27# 0.185 {NAD+}  (#27# 33°C <74>) <74>
KM	#27# 0.136 {NAD+}  (#27# 23°C <74>) <74>
KM	#27# 25 {ethanol}  (#27# 27°C <74>) <74>
KM	#27# 0.155 {NAD+}  (#27# 27°C <74>) <74>
KM	#27# 30 {ethanol}  (#27# 33°C <74>) <74>
KM	#27# 0.224 {NAD+}  (#27# 43°C <74>) <74>
KM	#27# 41.3 {ethanol}  (#27# 43°C <74>) <74>
KM	#30# 0.013 {acetaldehyde}  (#30# 70°C, pH 9.0, 50 mM Tris-HCl, 4 M
	NaCl <181>) <181>
KM	#30# 0.34 {ethanol}  (#30# 40°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl
	<181>) <181>
KM	#30# 0.059 {acetaldehyde}  (#30# 40°C, pH 9.0, 50 mM Tris-HCl, 4 M
	NaCl <181>) <181>
KM	#33# 29.9 {ethanol}  <135>
KM	#35# 0.03 {n-butanol}  (#35# isoenzyme BB-ADH <95>) <95>
KM	#35# 0.05 {all-trans-retinol}  (#35# isoenzyme AA-ADH <95>) <95>
KM	#35# 0.05 {12-hydroxydodecanoate}  (#35# isoenzyme BB-ADH and isoenzyme
	ADH-TT <95>) <95>
KM	#35# 0.06 {12-hydroxydodecanoate}  (#35# isoenzyme AA-ADH <95>) <95>
KM	#35# 0.26 {n-Hexanol}  (#35# isoenzyme TT-ADH <95>) <95>
KM	#35# 0.04 {Cyclohexanol}  (#35# isoenzyme BB-ADH <95>) <95>
KM	#35# 0.04 {n-Hexanol}  (#35# isoenzyme BB-ADH <95>) <95>
KM	#35# 0.5 {ethanol}  (#35# isoenzyme AA-ADH <95>) <95>
KM	#35# 0.02 {all-trans-retinol}  (#35# isoenzyme TT-ADH <95>) <95>
KM	#35# 0.02 {n-Hexanol}  (#35# isoenzyme TT-ADH <95>) <95>
KM	#35# 0.02 {12-hydroxydodecanoate}  (#35# isoenzyme BB-ADH <95>) <95>
KM	#35# 0.07 {n-butanol}  (#35# isoenzyme AA-ADH <95>) <95>
KM	#35# 2.3 {12-hydroxydodecanoate}  (#35# isoenzyme TT-ADH <95>) <95>
KM	#35# 0.76 {Cyclohexanol}  (#35# isoenzyme AA-ADH <95>) <95>
KM	#35# 2.6 {n-butanol}  (#35# isoenzyme TT-ADH <95>) <95>
KM	#35# 320 {Cyclohexanol}  (#35# isoenzyme TT-ADH <95>) <95>
KM	#37# 0.076 {NAD+}  <85>
KM	#37# 0.194 {acetaldehyde}  <85>
KM	#37# 4.68 {ethanol}  <85>
KM	#37,45# 0.036 {NADH}  <70,85>
KM	#4# 0.26 {NAD+}  <64>
KM	#4# 0.86 {butan-2-ol}  <64>
KM	#4# 1.87 {propan-2-ol}  <64>
KM	#4# 3.31 {butan-1-ol}  <64>
KM	#4# 3.42 {propan-2-ol}  <64>
KM	#4# 8.92 {ethanol}  <64>
KM	#4,5,8,10,18,40,70,74,77,81,84,89# -999 {more}  (#40,70# kinetics
	<117,121>; #10# pH-dependence of Km-value <89>; #4,74# kinetics of
	ethanol oxidation <63>; #40# kinetics of native and modified enzyme
	with coenzyme analogues <54>; #40# Km-values of active-site
	Co(II)substituted enzyme <31>; #8# Km values for the class I isoenzymes
	with the substrates ethanol, methanol, ethylene glycol, benzyl alcohol,
	octanol, cyclohexanol and 16-hydroxyhexadecanoic acid <13>; #8#
	steady-state kinetics <116>; #40# detailed kinetic mechanism,
	steady-state kinetics for wild-type and mutant enzymes, investigation
	of pH-dependency <111>; #77# detailed kinetics, computational analysis
	of the reaction mechanism <130>; #5# Km for isozymes ADH1, and ADH4 for
	all retinoid substrates in forward and reverse reaction <119>; #8# Km
	for isozymes ADH1B1, ADH1B2, and ADH4 for all retinoid substrates in
	forward and reverse reaction <119>; #84,89# Michaelis-Menten kinetics
	<105,226>; #8# steady-state kinetics, kinetic mechanism <124>; #8#
	steady-state kinetics, MW 25 kDa <115>; #10# wild-type and mutant forms
	of the 3 isozymes, steady-state kinetics, detailed kinetic analysis, at
	different pH values and temperatures <120>; #5# effects of
	tert-butanol, butyramide, valeramide and capronamide on KM-value for
	ethanol <141>)
	<13,22,23,31,54,63,75,83,89,105,111,115,116,117,119,120,121,124,130,141
	226>
KM	#40# 0.03 {Hexanol}  <42>
KM	#40# 0.06 {Butyraldehyde}  <42>
KM	#40# 0.16 {9-cis-retinal}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 0.3 {9-cis-retinol}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 0.3 {acycloNAD+}  (#40# substrate butan-1-ol, pH 8.0, 25°C <275>)
	<275>
KM	#40# 0.18 {(S)-2-octanol}  <31>
KM	#40# 0.26 {all-trans-retinal}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 0.003 {5beta-androstan-3beta-ol-17-one}  (#40# pH 7.3, 37°C,
	recombinant enzyme <116>) <116>
KM	#40# 0.012 {hexaldehyde}  <42>
KM	#40# 0.008 {5beta-cholanic acid-3-one}  (#40# pH 7.3, 37°C,
	recombinant enzyme <116>) <116>
KM	#40# 7 {ethanol}  (#40# pH 10.0 <28>) <28>
KM	#40# 0.11 {13-cis-retinal}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 0.2 {11-cis-retinal}  (#40# reduction with NADH <93>) <93>
KM	#40# 0.28 {11-cis-retinol}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 0.137 {13-cis-retinal}  (#40# reduction with NADH <93>) <93>
KM	#40# 0.011 {5beta-androstan-17beta-ol-3-one}  (#40# pH 7.3, 37°C,
	recombinant enzyme <116>) <116>
KM	#40# 1.5 {cinnamyl alcohol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 0.046 {benzyl alcohol}  <42>
KM	#40# 0.33 {acycloNAD+}  (#40# substrate hexan-1-ol, pH 8.0, 25°C
	<275>; #40# substrate propan-1-ol, pH 8.0, 25°C <275>) <275>
KM	#40# 0.39 {allyl alcohol}  (#40# pH 7.3, 37°C <117>) <117>
KM	#40# 0.34 {all-trans-retinal}  (#40# reduction with NADH <93>) <93>
KM	#40# 0.36 {acycloNAD+}  (#40# substrate ethanol, pH 8.0, 25°C <275>)
	<275>
KM	#40# 0.71 {crotyl alcohol}  (#40# pH 7.3, 37°C <117>) <117>
KM	#40# 9 {Isopropanol}  <31>
KM	#40# 0.031 {3-oxo-5beta-androstan-17beta-ol}  <42>
KM	#40# 0.091 {butanol}  <42>
KM	#40# 1.6 {3-Pentanol}  <31>
KM	#40# 0.059 {all-trans-retinol}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 0.73 {(S)-2-pentanol}  <31>
KM	#40# 14 {cyclohexanone}  <28>
KM	#40# 40 {ethanol}  <42>
KM	#40# 0.047 {5beta-Pregnan-21-ol-3,20-dione hemisuccinate}  <42>
KM	#40# 0.61 {acycloNAD+}  (#40# substrate benzyl alcohol, pH 8.0, 25°C
	<275>) <275>
KM	#40# 2.9 {Propanol}  <42>
KM	#40# 6 {acetaldehyde}  <28,42>
KM	#40# 15 {2-butanone}  <31>
KM	#40# 1.35 {(S)-2-butanol}  <31>
KM	#40# 6.7 {4-Methyl-1-pentanol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 7.5 {(R)-2-butanol}  <31>
KM	#40# 1.24 {propionaldehyde}  <42>
KM	#40# 42 {ethanol}  (#40# pH 7.0 <28>) <28>
KM	#40# 6.5 {Hexanol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 75 {3-Pentanone}  <31>
KM	#40# 2.46 {ethanol}  (#40# pH 7.3, 37°C <117>) <117>
KM	#40# 0.148 {benzaldehyde}  <42>
KM	#40# 13.4 {ethanol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 0.242 {9-cis-retinal}  (#40# reduction with NADH <93>) <93>
KM	#40# 14.1 {cyclohexanone}  <42>
KM	#40# 11.8 {Pentanol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 29.4 {butanol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 1.92 {(R)-2-octanol}  <31>
KM	#40# 13.6 {Propanol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 14.2 {2-Pentanone}  <31>
KM	#40# 13.8 {Hexanol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 0.257 {13-cis-retinol}  (#40# oxidation with NAD+ <93>) <93>
KM	#40# 4.58 {cinnamyl alcohol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 31.7 {(R)-2-pentanol}  <31>
KM	#40# 43.9 {Propanol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 53.8 {4-Methyl-1-pentanol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 53.9 {butanol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 56.2 {Pentanol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 93.3 {butan-2-ol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40# 118 {ethanol}  (#40# pH 6.1 <28>) <28>
KM	#40# 135 {acetone}  <31>
KM	#40# 193 {propan-2-ol}  (#40# mutant enzyme W54L <92>) <92>
KM	#40# 268 {2-propanol}  (#40# wilde-type enzyme ADh1 <92>) <92>
KM	#40,78# 4 {ethanol}  (#78# pyrazole-insensitive enzyme, pH 7.5 <24>;
	#40# wild-type enzyme Adh1 <92>) <24,92>
KM	#41# 1.3 {acetaldehyde}  (#41# enzyme form ADH II <68>) <68>
KM	#41# 0.012 {NADH}  (#41# enzyme form ADH II <68>) <68>
KM	#41# 0.027 {NADH}  (#41# enzyme form ADH I <68>) <68>
KM	#41# 0.11 {NAD+}  (#41# enzyme form ADH II <68>) <68>
KM	#41# 0.086 {acetaldehyde}  (#41# enzyme form ADH I <68>) <68>
KM	#41# 4.8 {ethanol}  (#41# enzyme form ADH I <68>) <68>
KM	#41# 0.073 {NAD+}  (#41# enzyme form ADH I <68>) <68>
KM	#41# 27 {ethanol}  (#41# enzyme form ADH II <68>) <68>
KM	#43# 0.17 {Valeraldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
KM	#43# 0.2 {acetophenone}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
KM	#43# 0.4 {acetophenone}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
KM	#43# 2 {Valeraldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
KM	#43# 0.25 {Capronaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
KM	#43# 0.28 {Valeraldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
KM	#43# 0.14 {4-chloroacetophenone}  (#43# pH 6.0, 37°C, recombinant
	enzyme expressed from Hansenula polymorpha <232>) <232>
KM	#43# 0.14 {Capronaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
KM	#43# 0.19 {phenylacetaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
KM	#43# 0.22 {Capronaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
KM	#43# 0.33 {phenylacetaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Hansenula polymorpha <232>) <232>
KM	#43# 0.66 {acetophenone}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Saccharomyces cerevisiae <232>) <232>
KM	#43# 0.91 {phenylacetaldehyde}  (#43# pH 6.0, 37°C, recombinant enzyme
	expressed from Arxula adeninivorans <232>) <232>
KM	#43# 0.53 {4-chloroacetophenone}  (#43# pH 6.0, 37°C, recombinant
	enzyme expressed from Saccharomyces cerevisiae <232>) <232>
KM	#43# 1.11 {4-chloroacetophenone}  (#43# pH 6.0, 37°C, recombinant
	enzyme expressed from Arxula adeninivorans <232>) <232>
KM	#44# 7.05 {acetaldehyde}  <6>
KM	#44# 31.1 {NADH}  <6>
KM	#44# 47.3 {ethanol}  <6>
KM	#44# 51.7 {NAD+}  <6>
KM	#45# 0.045 {Cyclohexanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
KM	#45# 0.05 {pentan-2-ol}  <66>
KM	#45# 0.3 {benzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5) containing
	0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at 55°C <153>)
	<153,163>
KM	#45# 0.26 {ethanol}  <66>
KM	#45# 0.26 {benzaldehyde}  (#45# mutant enzyme N249Y, at 65°C <154>)
	<154>
KM	#45# 0.6 {1-propanol}  (#45# wild type enzyme, at 65°C <154>) <154>
KM	#45# 0.6 {2-propanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
KM	#45# 1.3 {Cyclopentanone}  <66>
KM	#45# 1.3 {4-methoxybenzylalcohol}  (#45# in the presence of 3 mM NAD+,
	in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
KM	#45# 0.013 {NADH}  (#45# wild type enzyme, at 65°C, in the presence of
	benzaldehyde <154>) <154>
KM	#45# 0.21 {NADH}  (#45# mutant enzyme N249Y, at 65°C, in the presence
	of benzaldehyde <154>) <154>
KM	#45# 0.5 {propan-2-ol}  <66>
KM	#45# 1.7 {1-propanol}  (#45# mutant enzyme N249Y, at 65°C <154>) <154>
KM	#45# 0.09 {Anisaldehyde}  <70>
KM	#45# 0.021 {2-Methylcyclohexanol}  <66>
KM	#45# 0.2 {benzaldehyde}  (#45# carboxymethylated enzyme, at 55°C
	<153>) <153>
KM	#45# 0.4 {4-bromobenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
KM	#45# 2 {benzyl alcohol}  (#45# carboxymethylated enzyme, at 55°C
	<153>) <153>
KM	#45# 0.12 {4-bromobenzyl alcohol}  (#45# native enzyme, at 55°C <153>)
	<153>
KM	#45# 0.12 {4-bromobenzylalcohol}  (#45# in the presence of 3 mM NAD+,
	in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
KM	#45# 0.25 {(+)-2-methylcyclohexanone}  <66>
KM	#45# 0.28 {4-carboxybenzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5)
	containing 0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at
	55°C <153>) <153,163>
KM	#45# 0.9 {3-bromobenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
KM	#45# 0.0025 {Anisaldehyde}  <66>
KM	#45# 0.14 {4-methoxybenzaldehyde}  (#45# in 50 mM Tris-HCl (pH 7.5)
	containing 0.2 mM NADH + H+, at 65°C <163>; #45# native enzyme, at
	55°C <153>) <153,163>
KM	#45# 0.14 {3-bromobenzyl alcohol}  (#45# native enzyme, at 55°C <153>)
	<153>
KM	#45# 0.14 {3-bromobenzylalcohol}  (#45# in the presence of 3 mM NAD+,
	in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
KM	#45# 0.8 {benzylalcohol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>) <163>
KM	#45# 1.4 {4-methoxybenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
KM	#45# 2.4 {1-propanol}  (#45# carboxymethylated enzyme, at 55°C <153>)
	<153>
KM	#45# 0.23 {Cyclohexanol}  (#45# carboxymethylated enzyme, at 55°C
	<153>) <153>
KM	#45# 0.23 {4-methoxybenzyl alcohol}  (#45# wild type enzyme, at 65°C
	<154>) <154>
KM	#45# 1.2 {3-Methoxybenzyl alcohol}  (#45# native enzyme, at 55°C
	<153>) <153>
KM	#45# 1.2 {3-methoxybenzylalcohol}  (#45# in the presence of 3 mM NAD+,
	in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>; #45# in the presence of
	5 mM benzylalcohol, in 0.1 M glycine-NaOH, pH 9.2, at 65°C <163>) <163>
KM	#45# 1.9 {Cyclohexanol}  (#45# mutant enzyme N249Y, at 65°C <154>)
	<154>
KM	#45# 3.3 {3-Methoxybenzyl alcohol}  (#45# carboxymethylated enzyme, at
	55°C <153>) <153>
KM	#45# 0.055 {butan-1-ol}  <66>
KM	#45# 0.33 {1-propanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <153,163>
KM	#45# 0.35 {butan-2-ol}  <66>
KM	#45# 0.024 {4-methoxybenzaldehyde}  (#45# wild type enzyme, at 65°C
	<154>) <154>
KM	#45# 0.86 {4-methoxybenzaldehyde}  (#45# mutant enzyme N249Y, at 65°C
	<154>) <154>
KM	#45# 14 {butan-2-one}  <66>
KM	#45# 0.019 {propan-1-ol}  <66>
KM	#45# 7.5 {3-methylbutan-2-one}  <66>
KM	#45# 1.24 {4-methoxybenzyl alcohol}  (#45# mutant enzyme N249Y, at
	65°C <154>) <154>
KM	#45# 0.225 {pentan-3-ol}  <66>
KM	#45# 53 {2-propanol}  (#45# carboxymethylated enzyme, at 55°C <153>)
	<153>
KM	#45# 27 {methanol}  <66>
KM	#45# 6.6 {acetone}  <66>
KM	#45# 12.4 {NAD+}  (#45# mutant enzyme N249Y, at 65°C, in the presence
	of benzyl alcohol <154>) <154>
KM	#45# 184 {ethanol}  (#45# carboxymethylated enzyme, at 55°C <153>)
	<153>
KM	#45,104# 0.03 {benzaldehyde}  (#45# wild type enzyme, at 65°C <154>;
	#104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at
	65°C <207>) <154,207>
KM	#45,104# 0.03 {Cyclohexanol}  (#45# wild type enzyme, at 65°C <154>;
	#104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at
	65°C <207>) <154,207>
KM	#45,104# 0.26 {benzyl alcohol}  (#45# wild type enzyme, at 65°C <154>;
	#104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at
	65°C <207>) <154,207>
KM	#45,104# 1.3 {4-methoxybenzyl alcohol}  (#45# native enzyme, at 55°C
	<153>; #104# mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH
	10.5), at 65°C <207>) <153,207>
KM	#45,104,118,141# 0.5 {NAD+}  (#45# carboxymethylated enzyme, at 55°C
	<153>; #45# wild type enzyme, at 65°C, in the presence of benzyl
	alcohol <154>; #104# wild type enzyme, in 0.1 M glycine-NaOH buffer (pH
	10.5), at 65°C <207>; #141# mutant A25Y, pH 7.0, 30°C <260>; #118#
	mutant Y25A/W49F/W167Y, 30°C, pH not specified in the publication
	<257>) <153,154,207,257,260>
KM	#45,118# 0.8 {benzyl alcohol}  (#45# native enzyme, at 55°C <153>;
	#118# mutant Y25A/W49F/W167Y, 30°C, pH not specified in the
	publication <257>) <153,257>
KM	#45,118# 1.5 {benzyl alcohol}  (#45# mutant enzyme N249Y, at 65°C
	<154>; #118# mutant W87A, pH 7.0, 30°C <260>) <154,260>
KM	#45,123# 0.04 {NADH}  (#45# carboxymethylated enzyme, at 55°C <153>;
	#123# 65°C, pH 5.0 <218>) <153,218>
KM	#45,52# 0.7 {ethanol}  (#45# in the presence of 3 mM NAD+, in 0.1 M
	glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at 55°C
	<153>) <59,153,163>
KM	#45,60,89# 0.03 {NADH}  (#89# pH 8.5 <105>; #60# isozyme ADH II, pH
	6.0, 25°C <113>; #45# in 50 mM Tris-HCl (pH 7.5) containing 0.25 mM
	benzaldehyde, at 65°C <163>; #45# native enzyme, at 55°C <153>)
	<105,113,153,163>
KM	#45,68# 0.013 {benzyl alcohol}  (#68# enzyme form ADH-2 <60>) <60,66>
KM	#46# 0.26 {phenylacetaldehyde}  <149>
KM	#46# 0.012 {benzyl alcohol}  <149>
KM	#46# 0.02 {(R)-2-phenylpropanol}  <149>
KM	#46# 0.025 {1-phenylethanol}  <149>
KM	#46# 0.033 {3-phenylpropanol}  <149>
KM	#46# 0.157 {(S)-2-phenylpropanol}  <149>
KM	#46# 0.864 {2-phenylpropionaldehyde}  <149>
KM	#47# 10.4 {ethanol}  (#47# pH 9.0, 60°C, recombinant enzyme <223>)
	<223>
KM	#47# 2.6 {acetaldehyde}  (#47# pH 8.0, 60°C, recombinant enzyme <223>)
	<223>
KM	#47# 11.5 {1,2-propanediol}  (#47# pH 8.0, 60°C, recombinant enzyme
	<223>) <223>
KM	#47# 26.7 {1,3-Propanediol}  (#47# pH 9.0, 60°C, recombinant enzyme
	<223>) <223>
KM	#47,60# 0.2 {NADH}  (#60# isozyme ADH I, pH 5.5, 25°C <113>; #47# pH
	8.0, 60°C, recombinant enzyme <223>) <113,223>
KM	#49# 0.06 {ethanol}  <135>
KM	#5# 1.9 {Hexanol}  (#5# recombinant isozyme ADH1, pH 10.5, 25°C <119>)
	<119>
KM	#5# 0.085 {Hexanol}  (#5# recombinant isozyme ADH1, pH 7.5, 25°C
	<119>) <119>
KM	#5# 0.006 {Hexanol}  (#5# recombinant isozyme ADH4, pH 7.5, 25°C
	<119>) <119>
KM	#5# 0.63 {Hexanol}  (#5# recombinant isozyme ADH4, pH 10.5, 25°C
	<119>) <119>
KM	#5# 0.83 {ethanol}  (#5# recombinant isozyme ADH1, pH 10.5, 25°C
	<119>) <119>
KM	#5# 0.48 {ethanol}  (#5# recombinant isozyme ADH1, pH 7.5, 25°C <119>)
	<119>
KM	#5# 255 {ethanol}  (#5# recombinant isozyme ADH4, pH 10.5, 25°C <119>)
	<119>
KM	#5# 1625 {ethanol}  (#5# recombinant isozyme ADH4, pH 7.5, 25°C <119>)
	<119>
KM	#50# 460 {ethanol}  (#50# pH 7.0, 30°C <279>) <279>
KM	#51# 0.487 {NAD+}  <82>
KM	#51# 0.195 {NAD+}  <82>
KM	#52# 40 {NAD+}  (#52# enzyme from liver <59>) <59>
KM	#52# 60 {NAD+}  (#52# enzyme from caecum <59>) <59>
KM	#54# 0.02 {NADH}  (#54# reduction of acetaldehyde <99>) <99>
KM	#54# 0.28 {propan-1-ol}  <99>
KM	#54# 1.8 {acetaldehyde}  <99>
KM	#54# 0.15 {ethanol}  <99>
KM	#54# 50 {formaldehyde}  <99>
KM	#56# 0.78 {methanol}  <147>
KM	#56# 1.65 {1,2-propanediol}  <147>
KM	#56# 3.09 {1-propanol}  <147>
KM	#56# 2.58 {glycerol}  <147>
KM	#56# 3.42 {2-propanol}  <147>
KM	#56# 5.38 {ethanol}  <147>
KM	#56# 4.46 {formaldehyde}  <147>
KM	#56# 7.72 {benzyl alcohol}  <147>
KM	#56# 25.78 {1-butanol}  <147>
KM	#57# 6.66 {ethanol}  <147>
KM	#57# 3.54 {1-propanol}  <147>
KM	#57# 18.6 {glycerol}  <147>
KM	#57# 9.69 {methanol}  <147>
KM	#57# 15.84 {1,2-propanediol}  <147>
KM	#57# 11.46 {2-propanol}  <147>
KM	#57# 19.96 {benzyl alcohol}  <147>
KM	#57# 19.93 {1-butanol}  <147>
KM	#6# 1 {ethyl benzoylformate}  (#6# 65°C <169>) <169>
KM	#6# 1 {ethyl oxo(phenyl)acetate}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 5.3 {alpha-tetralol}  (#6# 65°C <169>) <169>
KM	#6# 5.8 {alpha-tetralone}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>)
	<169>
KM	#6# 0.035 {NADH}  (#6# 65°C <169>) <169>
KM	#6# 2.7 {methylbenzoylformate}  (#6# 65°C <169>) <169>
KM	#6# 2.7 {methyl oxo(phenyl)acetate}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 4.2 {(S)-1-indanol}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 4.2 {(S)-alpha-tetralol}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 4.2 {(S)-(+)-1-indanol}  (#6# 65°C <169>) <169>
KM	#6# 4.2 {(S)-(+)-alpha-tetraol}  (#6# 65°C <169>) <169>
KM	#6# 0.0035 {NADH}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 0.24 {NAD+}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>) <169>
KM	#6# 5.1 {1-Indanol}  (#6# 65°C <169>) <169>
KM	#6# 4.4 {4-methoxybenzaldehyde}  (#6# pH 6.0, 65°C <169>) <169>
KM	#6# 4.4 {3-Methoxybenzaldehyde}  (#6# 65°C <169>) <169>
KM	#6# 5.9 {1-phenyl-1,2-propanedione}  (#6# 65°C <169>) <169>
KM	#6# 5.9 {1-phenyl-1,2-propandione}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 11.2 {2,2,2-trifluoroacetophenone}  (#6# 65°C <169>; #6# pH 10.5,
	65°C <169>) <169>
KM	#6# 61 {4-methoxybenzyl alcohol}  (#6# 65°C <169>; #6# pH 10.5, 65°C
	<169>) <169>
KM	#6# 18.1 {(S)-1-phenylethanol}  (#6# pH 10.5, 65°C <169>) <169>
KM	#6# 18.1 {(S)-(-)-1-phenylethanol}  (#6# 65°C <169>) <169>
KM	#6# 27.6 {1-Indanone}  (#6# 65°C <169>; #6# pH 10.5, 65°C <169>) <169>
KM	#60# 0.3 {acetaldehyde}  (#60# isozyme ADH I, pH 5.5, 25°C <113>) <113>
KM	#60# 24 {acetaldehyde}  (#60# isozyme ADH II, pH 6.0, 25°C <113>) <113>
KM	#60# 1.2 {NAD+}  (#60# isozyme ADH I, pH 8.5, 25°C <113>) <113>
KM	#60# 2.3 {ethanol}  (#60# isozyme ADH I, pH 8.5, 25°C <113>) <113>
KM	#60# 7.3 {ethanol}  (#60# isozyme ADH II, pH 8.5, 25°C <113>) <113>
KM	#65# 8.7 {ethanol}  <135>
KM	#67# 0.11 {NADH}  <69>
KM	#67# 0.125 {NAD+}  <69>
KM	#67# 22.2 {ethanol}  <69>
KM	#68# 0.04 {12-hydroxydodecanoate}  (#68# enzyme form ADH-3 <60>) <60>
KM	#68# 0.2 {pentan-1-ol}  (#68# enzyme form ADH-3 <60>) <60>
KM	#68# 2 {butan-1-ol}  (#68# enzyme form ADH-3 <60>) <60>
KM	#68# 0.23 {NAD+}  (#68# oxidation of ethanol <60>) <60>
KM	#68# 0.011 {octan-1-ol}  (#68# enzyme form ADH-3 <60>) <60>
KM	#68# 0.0051 {NADH}  (#68# reduction of octanal <60>) <60>
KM	#68# 0.043 {octanal}  (#68# enzyme form ADH-2 <60>) <60>
KM	#68# 5.2 {Cyclohexanol}  (#68# enzyme form ADH-3 <60>) <60>
KM	#68# 8.1 {ethanol}  (#68# enzyme form ADH-3 <60>) <60>
KM	#69# 0.17 {NAD+}  <84>
KM	#69# 0.021 {NADH}  <84>
KM	#69# 2.5 {ethanol}  <84>
KM	#69# 0.0086 {acetaldehyde}  <84>
KM	#69# 64 {ethanol}  <84>
KM	#69# 64 {propan-2-ol}  <84>
KM	#7,8# 10.6 {ethanol}  (#8# recombinant allozyme Val308, pH 7.5, 25°C
	<115>) <115,135>
KM	#71# 1.6 {butan-2-ol}  <64>
KM	#71# 1.99 {propan-2-ol}  <64>
KM	#71# 4.16 {propan-2-ol}  <64>
KM	#71# 6.44 {ethanol}  <64>
KM	#74# 0.41 {butan-2-ol}  <64>
KM	#74# 0.19 {NAD+}  <64>
KM	#74# 3.33 {propan-2-ol}  <64>
KM	#74# 0.93 {propan-2-ol}  <64>
KM	#74# 3.01 {butan-1-ol}  <64>
KM	#74# 5.22 {ethanol}  <64>
KM	#77# 1 {cis-4-methylcyclohexanol}  <61>
KM	#77# 0.028 {NAD+}  (#77# oxidation of propan-2-ol <61>) <61>
KM	#77# 0.011 {NAD+}  (#77# oxidation of ethanol <61>) <61>
KM	#77# 1.2 {R-(+)-cis-verbenol}  <61>
KM	#77# 1.5 {R-(+)-trans-bicyclo(2.2.1)-heptanol}  <61>
KM	#77# 1.9 {butan-1-ol}  <61>
KM	#77# 1.9 {propan-1-ol}  <61>
KM	#77# 0.81 {4-methylpentan-1-ol}  <61>
KM	#77# 1.1 {2-propanol}  <61>
KM	#77# 1.1 {trans-4-methylcyclohexanol}  <61>
KM	#77# 2.7 {2-methylpropan-1-ol}  <61>
KM	#77# 0.85 {S-(-)-trans-bicyclo(2.2.1)-heptanol}  <61>
KM	#77# 4.1 {pentan-1-ol}  <61>
KM	#77# 3.9 {S-(-)-1-phenylethanol}  <61>
KM	#77# 3.4 {R-(+)-1-phenylethanol}  <61>
KM	#77# 6 {ethanol}  <61>
KM	#77# 3.8 {S-(-)-cis-bicyclo(2.2.1)-heptanol}  <61>
KM	#77# 0.95 {S-(-)-2-methylbutan-1-ol}  <61>
KM	#77# 7.4 {hexan-1-ol}  <61>
KM	#77# 6.2 {ethanol}  <61>
KM	#77# 6.6 {heptan-4-ol}  <61>
KM	#77# 0.72 {Cyclohexanol}  <61>
KM	#78# 0.06 {butanol}  (#78# pyrazole-insensitive enzyme, pH 7.5 <24>)
	<24>
KM	#78# 0.1 {acetaldehyde}  (#78# pyrazole-sensitive enzyme, pH 7.0 <24>)
	<24>
KM	#78# 0.18 {ethanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>) <24>
KM	#78# 0.012 {butanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>) <24>
KM	#78# 0.012 {Pentanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>)
	<24>
KM	#78# 0.018 {Pentanol}  (#78# pyrazole-sensitive enzyme, pH 10.0 <24>)
	<24>
KM	#78# 0.02 {butanol}  (#78# pyrazole-sinensitive enzyme, pH 10.0 <24>)
	<24>
KM	#78# 0.09 {butanol}  (#78# pyrazole-sensitive enzyme, pH 10.0 <24>) <24>
KM	#78# 12 {methanol}  (#78# pyrazole-sensitive enzyme, pH 7.5 <24>) <24>
KM	#78# 5 {ethanol}  (#78# pyrazole-insensitive enzyme, pH 10.0 <24>) <24>
KM	#78# 14 {methanol}  (#78# pyrazole-sensitive enzyme, pH 10.0 <24>) <24>
KM	#78# 11.5 {acetaldehyde}  (#78# pyrazole-insensitive enzyme, pH 7.0
	<24>) <24>
KM	#8# 0.06 {16-hydroxyhexadecanoate}  <14>
KM	#8# 0.063 {NAD+}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C
	<115>) <115>
KM	#8# 0.55 {1-Octanol}  <11>
KM	#8# 0.004 {4-hydroxy-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B1
	<107>) <107>
KM	#8# 0.012 {all-trans-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B2
	<107>) <107>
KM	#8# 0.012 {retinol}  (#8# recombinant allozyme Val308, pH 7.5, 25°C
	<115>) <115>
KM	#8# 0.008 {Cyclohexanol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
KM	#8# 0.013 {NAD+}  (#8# isoenzyme alpha,alpha <16,17>) <16,17>
KM	#8# 0.049 {ethanol}  (#8# isoenzyme beta1,beta1 <17>) <15,17>
KM	#8# 0.015 {4-hydroxy-retinol}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
KM	#8# 0.018 {11-cis-retinol}  (#8# isozyme ADH1B2, pH 7.5, 25°C <119>)
	<119>
KM	#8# 0.022 {NAD+}  <12>
KM	#8# 0.027 {5beta-Pregnan-3beta-ol-20-one}  (#8# pH 7.3, 37°C, ADH1C*2
	(gamma2gamma2) <116>) <116>
KM	#8# 0.027 {4-oxo-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B2 <107>)
	<107>
KM	#8# 0.032 {3-Phenyl-1-propanol}  <14>
KM	#8# 0.09 {Pentanol}  <14>
KM	#8# 0.025 {NAD+}  <16>
KM	#8# 0.025 {4-oxo-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B1 <107>)
	<107>
KM	#8# 0.025 {3,4-dihydro-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B2
	<107>) <107>
KM	#8# 0.2 {tryptophol}  <14>
KM	#8# 1 {ethanol}  (#8# isoenzyme gamma1,gamma1 <15>) <15>
KM	#8# 0.009 {all-trans-retinol}  <53>
KM	#8# 0.009 {Octanol}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C
	<115>) <115>
KM	#8# 0.023 {all-trans-retinol}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
KM	#8# 0.023 {9-cis-retinol}  (#8# isozyme ADH1B2, pH 7.5, 25°C <119>)
	<119>
KM	#8# 0.25 {5beta-cholanic acid-3-one}  (#8# pH 7.3, 37°C, ADH1C*2
	(gamma2gamma2) <116>) <116>
KM	#8# 0.28 {Pentanol}  <53>
KM	#8# 0.0025 {NADH}  <16>
KM	#8# 0.8 {Octanol}  <21>
KM	#8# 2.4 {octanal}  <16>
KM	#8# 1.8 {ethanol}  <10>
KM	#8# 0.23 {12-hydroxydodecanoate}  <14>
KM	#8# 0.028 {3,4-dihydro-retinol}  (#8# pH 7.5, 25°C, isozyme ADH4
	<107>) <107>
KM	#8# 0.15 {benzyl alcohol}  <96>
KM	#8# 0.0036 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	ADH1C*2 (gamma2gamma2) <116>) <116>
KM	#8# 0.0036 {5beta-pregnan-3,20-dione}  (#8# pH 7.3, 37°C, ADH1C*2
	(gamma2gamma2) <116>) <116>
KM	#8# 0.011 {NADH}  (#8# isoenzyme alpha,alpha <16>) <16>
KM	#8# 0.011 {all-trans-retinal}  (#8# pH 7.5, 25°C, isozyme ADH1B1
	<107>) <107>
KM	#8# 0.011 {retinol}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C
	<115>) <115>
KM	#8# 0.011 {9-cis-retinol}  (#8# isozyme ADH1B1, pH 7.5, 25°C <119>)
	<119>
KM	#8# 0.011 {4-hydroxy-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B2
	<107>) <107>
KM	#8# 1.2 {Octanol}  <16>
KM	#8# 4.3 {acetaldehyde}  (#8# isoenzyme alpha,alpha <15>) <15>
KM	#8# 0.007 {NADH}  (#8# isoenzyme gamma1,gamma1 <16>) <16>
KM	#8# 0.007 {benzyl alcohol}  <14>
KM	#8# 0.007 {Octanol}  <14>
KM	#8# 0.033 {all-trans-retinol}  (#8# isozyme ADH1B2, pH 7.5, 25°C
	<119>; #8# pH 7.5, 25°C, isozyme ADH1B2 <107>) <107,119>
KM	#8# 0.034 {all-trans-retinal}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>)
	<107>
KM	#8# 0.034 {Vanillyl alcohol}  <14>
KM	#8# 0.08 {Octanol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
KM	#8# 0.085 {acetaldehyde}  (#8# isoenzyme beta1,beta1 <15,20>) <15,20>
KM	#8# 0.84 {ethanol}  (#8# isoenzyme beta2,beta2 <20>) <20>
KM	#8# 0.017 {4-oxo-retinal}  (#8# pH 7.5, 25°C, isozyme ADH4 <107>) <107>
KM	#8# 0.046 {5beta-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	ADH1C*2 (gamma2gamma2) <116>) <116>
KM	#8# 0.33 {acetaldehyde}  (#8# isoenzyme gamma1,gamma1 <15>) <15>
KM	#8# 0.13 {Hexanol}  <53>
KM	#8# 0.34 {NAD+}  <96>
KM	#8# 0.024 {3,4-dihydro-retinol}  (#8# pH 7.5, 25°C, isozyme ADH1B2
	<107>) <107>
KM	#8# 0.035 {11-cis-retinol}  (#8# isozyme ADH1B1, pH 7.5, 25°C <119>)
	<119>
KM	#8# 0.048 {12-hydroxydodecanoate}  <53>
KM	#8# 9 {ethanol}  (#8# recombinant allozyme Ile308, pH 7.5, 25°C <115>)
	<115>
KM	#8# 17 {Hexanol}  <21>
KM	#8# 0.026 {3,4-dihydro-retinal}  (#8# pH 7.5, 25°C, isozyme ADH4
	<107>) <107>
KM	#8# 0.63 {ethanol}  (#8# isoenzyme gamma2,gamma2 <15>) <15>
KM	#8# 11 {Vanillyl alcohol}  <16>
KM	#8# 1.6 {ethanol}  (#8# isoenzyme beta1,beta1 <17>) <17>
KM	#8# 4.2 {ethanol}  (#8# isoenzyme alpha,alpha <15,17>) <15,17>
KM	#8# 0.016 {Octanol}  (#8# recombinant allozyme Val308, pH 7.5, 25°C
	<115>) <115>
KM	#8# 0.056 {12-Hydroxydodecanoic acid}  <11>
KM	#8# 0.91 {Propanol}  <96>
KM	#8# 50 {ethylene glycol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
KM	#8# 260 {NADH}  (#8# isoenzyme beta3,beta3 <20>) <20>
KM	#8# 0.047 {12-hydroxydodecanoate}  <96>
KM	#8# 150 {methanol}  (#8# isoenzyme alpha,gamma1 <13>) <13>
KM	#8# 0.24 {acetaldehyde}  (#8# isoenzyme gamma2,gamma2 <15>; #8#
	isoenzymes beta2,beta2 <15,20>) <15,20>
KM	#8# 0.24 {butanol}  <96>
KM	#8# 0.94 {ethanol}  (#8# isoenzyme beta2,beta2 <15>) <15>
KM	#8# 10.4 {methanol}  <12>
KM	#8# 3.4 {acetaldehyde}  (#8# isoenzyme beta3,beta3 <20>) <20>
KM	#8# 6.4 {NADH}  (#8# isoenzyme beta1,beta1 <20>) <20>
KM	#8# 0.044 {Pentanol}  <96>
KM	#8# 0.058 {5beta-androstan-3beta-ol-17-one}  (#8# pH 7.3, 37°C,
	ADH1C*2 (gamma2gamma2) <116>) <116>
KM	#8# 0.0064 {NADH}  (#8# isoenzyme beta1,beta1 <16>) <16>
KM	#8# 36 {ethanol}  (#8# isoenzyme beta3,beta3 <20>) <20>
KM	#8# 120 {ethanol}  <14>
KM	#8# 120 {(S)-2-butanol}  <53>
KM	#8# 7.4 {NAD+}  (#8# isoenzyme beta1,beta1 <20>) <20>
KM	#8# 18 {ethanol}  <96>
KM	#8# 23 {Cyclohexanol}  (#8# isoenzyme beta1,beta1 <13>) <13>
KM	#8# 3.2 {ethanol}  (#8# isoenzyme gamma1,gamma1 <17>) <17,211>
KM	#8# 27 {1-Pentanol}  <11>
KM	#8# 210 {Cyclohexanol}  <14>
KM	#8# 290 {ethylene glycol}  <14>
KM	#8# 0.0074 {NAD+}  (#8# isoenzyme beta1,beta1 <17>; #8# isoenzyme
	beta2,beta2 <16>) <16,17>
KM	#8# 0.0087 {NAD+}  (#8# isoenzyme gamma2,gamma2 <16,17>) <16,17>
KM	#8# 0.79 {butanol}  <53>
KM	#8# 180 {NAD+}  (#8# isoenzyme beta2,beta2 <20>) <20>
KM	#8# 310 {2-deoxy-D-ribose}  <14>
KM	#8# 1.39 {Propanol}  <53>
KM	#8# 0.0079 {NAD+}  (#8# isoenzyme gamma1,gamma1 <16,17>) <16,17>
KM	#8# 105 {NADH}  (#8# isoenzyme beta2,beta2 <20>) <20>
KM	#8# 560 {2-propanol}  <14>
KM	#8# 710 {NAD+}  (#8# isoenzyme beta3,beta3 <20>) <20>
KM	#8,118# 1.5 {ethanol}  (#8# isoenzyme alpha,alpha <17>; #118# mutant
	C257L, pH 8.0, 60°C <246>) <17,246>
KM	#8,12,126# 0.45 {ethanol}  (#12# pH 10.8 <45>; #126# pH 9.0, 22°C,
	recombinant enzyme <222>) <12,45,222>
KM	#8,123# 0.18 {NAD+}  (#8# isoenzyme beta1,beta1 <16>; #123# 65°C, pH
	10.5 <218>) <16,218>
KM	#8,149# 0.105 {NADH}  (#8# isoenzyme beta2,beta2 <16>; #149#
	cosubstrate acetoin, pH 6.0, 70°C <243>) <16,243>
KM	#8,16# 1.7 {ethanol}  (#16# isoenzyme III <79>; #8# isoenzyme
	alpha,gamma1 <13>; #8# isoenzyme gamma2,gamma2 <17>) <13,17,79>
KM	#8,30# 0.022 {ethanol}  (#8# isoenzyme beta1,beta1 <20>; #30# 70°C, pH
	9.0, 50 mM Tris-HCl, 4 M NaCl <181>) <20,181>
KM	#8,35# 0.03 {all-trans-retinol}  (#35# isoenzyme BB-ADH <95>; #8#
	isozyme ADH1B1, pH 7.5, 25°C <119>; #8# pH 7.5, 25°C, isozyme ADH1B1
	<107>) <95,107,119>
KM	#8,35# 28 {ethanol}  (#35# isoenzyme TT-ADH <95>) <53,95>
KM	#8,54# 0.074 {NAD+}  (#54# oxidation of ethanol <99>; #8# recombinant
	allozyme Val308, pH 7.5, 25°C <115>) <99,115>
KM	#8,9# 0.1 {12-hydroxydodecanoate}  (#9# isoenzyme ADH-1, pH 10.0 <49>)
	<16,49>
KM	#82# 0.0014 {Octanol}  <101>
KM	#82# 0.0007 {Hexanol}  <101>
KM	#82# 0.35 {butanol}  <101>
KM	#82# 0.39 {Cyclohexanol}  <101>
KM	#82# 5 {methanol}  <101>
KM	#82# 1.23 {ethanol}  <101>
KM	#84# 5.3 {ethyl pyruvate}  (#84# pH 6.5, 50°C, recombinant enzyme
	<226>) <226>
KM	#87# 24.2 {ethanol}  (#87# pH 10.0, 50°C <118>) <118>
KM	#89# 1.9 {acetaldehyde}  (#89# pH 8.5 <105>) <105>
KM	#89# 1.12 {NAD+}  (#89# pH 8.5 <105>) <105>
KM	#9# 0.05 {benzyl alcohol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
KM	#9# 0.057 {NAD+}  (#9# isoenzyme 1 <51>) <51>
KM	#9# 0.1 {1-Octanol}  (#9# isoenzyme ADH-2 <49>) <49>
KM	#9# 0.16 {3beta,12alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 3
	<51>) <51>
KM	#9# 0.16 {3beta,7alpha,12alpha-trihydroxy-5beta-cholanoate}  (#9#
	isoenzyme 2 <51>) <51>
KM	#9# 0.17 {1-butanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
KM	#9# 0.3 {octanal}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9# 0.31 {acetaldehyde}  (#9# isoenzyme 1 <51>) <51>
KM	#9# 0.31 {3beta,12alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme I
	<51>) <51>
KM	#9# 0.013 {12-hydroxydodecanoate}  (#9# isoenzyme ADH-3, pH 10.0 <49>)
	<49>
KM	#9# 0.04 {5alpha-androstan-17beta-ol-3-one}  (#9# isoenzyme 1 <51>) <51>
KM	#9# 0.217 {acetaldehyde}  (#9# isoenzyme 3 <51>) <51>
KM	#9# 0.5 {1-Octanol}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9# 0.027 {5alpha-androstan-17beta-ol-3-one}  (#9# isoenzyme 4 <51>)
	<51>
KM	#9# 0.032 {3beta-7alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 3
	<51>) <51>
KM	#9# 0.021 {5alpha-androstan-17beta-ol-3-one}  (#9# isoenzyme 2 <51>)
	<51>
KM	#9# 0.025 {1-Octanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
KM	#9# 0.025 {5alpha-androstan-17beta-ol-3-one}  (#9# isoenzyme 2 <51>)
	<51>
KM	#9# 0.25 {NAD+}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 2.2 {Cyclohexanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
KM	#9# 0.14 {5beta-androstan-3beta-ol-17 one}  (#9# isoenzyme 3 <51>) <51>
KM	#9# 0.182 {3beta,7alpha,12alpha-trihydroxy-5beta-cholanoate}  (#9#
	isoenzyme 3 <51>) <51>
KM	#9# 1.4 {ethanol}  (#9# isoenzyme ADH-3, pH 10.0 and pH 7.5 <49>) <49>
KM	#9# 1.4 {benzyl alcohol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 1.4 {12-hydroxydodecanoate}  (#9# isoenzyme ADH-1, pH 10.0 <49>)
	<49>
KM	#9# 1.4 {m-nitrobenzaldehyde}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9# 3.1 {1-Pentanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 0.23 {acetaldehyde}  (#9# isoenzyme 2 <51>) <51>
KM	#9# 0.0017 {NADH}  (#9# isoenzyme ADH-2, pH 7.5 <49>) <49>
KM	#9# 2.5 {2-Buten-1-ol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 3 {Butanal}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9# 0.08 {1-Pentanol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
KM	#9# 0.125 {5beta-androstan-3beta-ol-17 one}  (#9# isoenzyme 2 <51>) <51>
KM	#9# 0.35 {2-Buten-1-ol}  (#9# isoenzyme ADH-3, pH 10.0 <49>) <49>
KM	#9# 0.35 {3beta,7alpha-12alpha-trihydroxy-5beta-cholanoate}  (#9#
	isoenzyme 4 <51>) <51>
KM	#9# 0.076 {NADH}  (#9# isoenzyme 1 <51>) <51>
KM	#9# 1.41 {ethanol}  (#9# isoenzyme 4 <51>) <51>
KM	#9# 0.071 {3beta-7alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 4
	<51>) <51>
KM	#9# 0.066 {3beta-7alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 1
	<51>) <51>
KM	#9# 17 {1-butanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 0.091 {NADH}  (#9# isoenzyme 3 <51>) <51>
KM	#9# 1.6 {Octanol}  (#9# isoenzyme ADH-2, pH 7.5 <49>) <49>
KM	#9# 3.5 {octanal}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9# 0.064 {3beta-7alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 2
	<51>) <51>
KM	#9# 0.115 {NAD+}  (#9# isoenzyme 2 <51>) <51>
KM	#9# 1.87 {ethanol}  (#9# isoenzyme 3 <51>) <51>
KM	#9# 60 {2-Buten-1-ol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
KM	#9# 0.044 {NAD+}  (#9# isoenzyme 4 <51>) <51>
KM	#9# 0.051 {NADH}  (#9# isoenzyme 4 <51>) <51>
KM	#9# 0.51 {1-Octanol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
KM	#9# 0.128 {3beta,12alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 2
	<51>) <51>
KM	#9# 220 {Cyclohexanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 230 {1-butanol}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9# 1.37 {ethanol}  (#9# isoenzyme 1 <51>) <51>
KM	#9# 0.248 {3beta,12alpha-dihydroxy-5beta-cholanoate}  (#9# isoenzyme 4
	<51>) <51>
KM	#9# 78 {1-Pentanol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
KM	#9# 0.123 {5beta-androstan-3beta-ol-17 one}  (#9# isoenzyme 4 <51>) <51>
KM	#9# 0.099 {NAD+}  (#9# isoenzyme 2 <51>) <51>
KM	#9# 0.149 {3beta,7alpha,12alpha-trihydroxy-5beta-cholanoate}  (#9#
	isoenzyme I <51>) <51>
KM	#9# 0.276 {acetaldehyde}  (#9# isoenzyme 4 <51>) <51>
KM	#9# 340 {ethanol}  (#9# isoenzyme ADH-1, pH 10.0 <49>) <49>
KM	#9# 0.164 {5beta-androstan-3beta-ol-17 one}  (#9# isoenzyme 1 <51>) <51>
KM	#9# 1900 {Cyclohexanol}  (#9# isoenzyme ADH-2, pH 10.0 <49>) <49>
KM	#9# 5000 {ethanol}  (#9# isoenzyme ADH-1, pH 7.5 <49>) <49>
KM	#9,132# 0.071 {NADH}  (#9# isoenzyme 2 <51>; #132# pH 6.0, temperature
	not specified in the publication <237>) <51,237>
KM	#9,35# 0.76 {ethanol}  (#9# isoenzyme 2 <51>; #35# isoenzyme BB-ADH
	<95>) <51,95>
KM	#9,45,71,118# 0.2 {NAD+}  (#9# isoenzyme ADH-1, pH 7.5 <49>; #45# in
	0.1 M glycine-NaOH, pH 9.2, at 65°C <163>; #45# native enzyme, at
	55°C <153>; #118# mutant W87A, pH 7.0, 30°C <260>) <49,64,153,163,260>
KM	#9,47# 0.05 {NAD+}  (#9# isoenzyme ADH-1, pH 7.5 <49>; #47# pH 9.0,
	60°C, recombinant enzyme <223>) <49,223>
KM	#9,60# 0.04 {NAD+}  (#9# isoenzyme ADH-2, pH 10.0 and pH 7.5 <49>; #60#
	isozyme ADH II, pH 8.5, 25°C <113>) <49,113>
KM	#9,66,80# 0.1 {NAD+}  (#9# isoenzyme ADH-3 <49>) <49,77,78,211>
KM	#9,78# 0.8 {ethanol}  (#78# pyrazole-sensitive enzyme, pH 10.0 <24>)
	<10,24>
KM	#91# 0.147 {ethanol}  (#91# 20°C, pH 9.0 <144>) <144>
KM	#91# 0.19 {ethanol}  (#91# 10°C, pH 9.0 <144>) <144>
KM	#91# 0.43 {ethanol}  (#91# 50°C, pH 9.0 <144>) <144>
KM	#91# 0.168 {ethanol}  (#91# 30°C, pH 9.0 <144>) <144>
KM	#91# 0.248 {ethanol}  (#91# 40°C, pH 9.0 <144>) <144>
KM	#91# 1.04 {ethanol}  (#91# 60°C, pH 9.0 <144>) <144>
KM	#92# 0.12 {NAD+}  (#92# 25°C, pH 7.0 <137>) <137>
KM	#92# 0.048 {NADH}  (#92# 25°C, pH 7.0 <137>) <137>
KM	#92# 57.5 {2-propanol}  (#92# 25°C, pH 7.0 <137>) <137>
KM	#92# 13.6 {phenyl trifluoromethyl ketone}  (#92# 25°C, pH 7.0 <137>)
	<137>
KM	#93# 0.19 {n-Propanol}  (#93# 2 mM zinc sulfate in 100 mM glycine-NaOH
	(pH 10.5) at 65°C <162>) <162>
KM	#93# 2.4 {iso-propanol}  (#93# 2 mM zinc sulfate in 100 mM glycine-NaOH
	(pH 10.5) at 65°C <162>) <162>
KM	#93# 1.33 {ethanol}  (#93# 2 mM zinc sulfate in 100 mM glycine-NaOH (pH
	10.5) at 65°C <162>) <162>
KM	#93# 0.44 {benzylalcohol}  (#93# 2 mM zinc sulfate in 100 mM
	glycine-NaOH (pH 10.5) at 65°C <162>) <162>
KM	#94# 0.0145 {benzylalcohol}  (#94# in 50 mM glycine-NaOH at pH 10.0
	<159>) <159>
KM	#94# 0.0172 {ethanol}  (#94# in 50 mM glycine-NaOH at pH 10.0 <159>)
	<159>
KM	#98# 0.056 {ethanol}  <173>
KM	#99# 0.59 {propanal}  (#99# 33°C, pH 7 <171>) <171>
KM	#99# 6.8 {ethanol}  (#99# 33°C, pH 8 <171>) <171>
KM	#99# 11.9 {2-butanol}  (#99# 33°C, pH 8 <171>) <171>
KM	#99# 0.92 {acetaldehyde}  (#99# 33°C, pH 7 <171>) <171>
KM	#99# 10.3 {n-Pentanal}  (#99# 33°C, pH 8 <171>) <171>
KM	#99# 2.01 {propanone}  (#99# 33°C, pH 7 <171>) <171>
KM	#99# 19.6 {2-propanol}  (#99# 33°C, pH 8 <171>) <171>
KM	#99# 35.1 {n-butanol}  (#99# 33°C, pH 8 <171>) <171>
KM	#99# 4.24 {Butanal}  (#99# 33°C, pH 7 <171>) <171>
KM	#99# 3.04 {methanol}  (#99# 33°C, pH 8 <171>) <171>
KM	#99# 7.49 {n-Propanol}  (#99# 33°C, pH 8 <171>) <171>

PH_OPTIMUM
PHO	#10# 8.3 (#10# alcohol dehydrogenase IV <87>) <87>
PHO	#10,41,43,44,50,55,68,150# 6.5 (#44# reduction of acetaldehyde <6>;
	#68# reduction of octanal <60>; #41# reduction of acetaldehyde, enzyme
	form ADH II <68>; #43# reduction <114>; #55# carbonyl reduction <255>;
	#150# reduction of crotonaldehyde <244>; #10# reduction of
	glycolaldehyde, furfural, formaldehyde, butyraldehyde, and
	propionaldehyde <285>) <6,60,68,114,244,255,279,285>
PHO	#10,67,104# 6.8 (#10# soluble enzyme <182>; #67# oxidation of NADH
	<69>; #104# for the reduction reaction with benzaldehyde <207>)
	<69,182,207>
PHO	#10,70,98# 7.8 (#10,70# assay at <121>) <121,173>
PHO	#100# 6-7 (#100# reduction of N-benzyl-3-pyrrolidinone <185>) <185>
PHO	#110,123# 5 (#123# ketone reduction reaction <218>) <213,218>
PHO	#122,123# 5.1 (#122# reduction reaction <219>; #123# reduction of
	ketones <219>) <219>
PHO	#127# 5.5-6 (#127# reduction reaction <225>) <225>
PHO	#13,18,30,43,45,47,104,111,126,149# 9 (#45# wild type enzyme <154>;
	#13# recombinant enzyme <126>; #104# assay at <235>; #18# oxidation of
	ethanol <97>; #47# ethanol oxidation <223>; #43# oxidation <114>; #126#
	alcohol oxidation <222>; #111# the optimal pH for oxidation is at a pH
	of 9.0 <197>; #149# oxidation reaction of alcohols <243>)
	<97,114,126,154,165,181,197,222,223,235,243>
PHO	#14# 8.1 (#14# reduction of propan-2-ol or ethanol <81>) <81>
PHO	#142# 6.1 (#142# reduction of ketones <138>) <138>
PHO	#149# 3 (#149# reduction of aldehydes <243>) <243>
PHO	#15# 3.8 (#15# -4.3 <134>) <134>
PHO	#16# 8.6-8.8 (#16# reduction of acetaldehyde, isoenzyme I <79>) <79>
PHO	#18# 8.7 <76>
PHO	#19,39# 6.7 (#19# reduction of acetaldehyde <71>) <71,131>
PHO	#21# 8.9 (#21# oxidation of ethanol <72>) <72>
PHO	#21,25# 5.7 (#21# reduction of acetaldehyde <72>) <72,188>
PHO	#26,40,142# 8.8 (#26# assay at <129>; #142# oxidation of secondary
	alcohols <138>; #40# activity for both free and immobilized HLAD
	increases with pH up to 8.8 <204>) <129,138,204>
PHO	#3,5,8,10,45,54,74# 7.5 (#5,8# assay at <107,124,200>; #54# reduction
	of acetaldehyde <99>; #3# reduction of substrate <4>; #74# and second
	optimum at pH 9.9 <64>; #45# reduction of anisaldehyde <66>; #8#
	kinetic analysis assay at <115>; #10# Zn-ADH, Co-ADH, and Cu-ADH <122>;
	#10# enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via
	glutaraldehyde <182>; #10# immobilized enzyme, at 25°C <196>; #8#
	assay at, class IV enzyme, reduction reaction <229>)
	<4,64,66,99,107,115,122,124,182,196,200,229>
PHO	#3,8,18,45,60,89,127# 8.5 (#3# oxidation of substrate <4>; #18#
	wild-type enzyme ADH1-1S <97>; #45# oxidation of benzyl alcohol <66>;
	#8# isoenzyme beta2,beta2 <20>; #127# oxidation reaction <225>; #60#
	assay at, forward reaction, ADH I and ADH II <113>; #8# isozyme ADH1B2,
	assay at <119>; #45# mutant enzyme N249Y <154>; #8# assay at, total ADH
	activity <229>) <4,20,66,97,105,113,119,154,225,229>
PHO	#37# 8-8.5 <85>
PHO	#4,8,18,24,40,47,71,113,114,118,131,135,150# 8 (#40# assay at <111>;
	#118# oxidation of ethanol <256>; #4,71# and a second optimum at pH 9.5
	<64>; #18# mutant enzyme ADH1-1S1108 <97>; #47# aldehyde reduction
	<223>; #8# assay at, class III enzyme, reduction reaction <229>; #131#
	reduction of 2-pentanone <239>; #150# oxidation of crotyl aclohol
	<244>) <64,97,106,111,215,223,229,239,244,252,256>
PHO	#4,9,23,41,44,54,71,92,104# 9.5 (#23# assay at <128>; #9,44,54#
	oxidation of ethanol <6,51,99>; #4,71# and a second optimum at pH 8.0
	<64>; #9# isoenzyme 1 <51>; #41# enzyme form ADH-I, oxidation of
	ethanol <67,68>; #92# oxidative reaction <137>; #104# for the oxidation
	reaction, ADH activity shows a slight dependence on pH, displaying a
	broad peak with a maximum around 9.5 <207>)
	<6,51,64,67,68,99,128,137,207>
PHO	#41,96# 4.5 (#41# reduction of acetaldehyde, enzyme form ADH I <68>)
	<68,168>
PHO	#42# 11.2 (#42# oxidation of ethanol, pyrazole-sensitive enzyme form
	<25>) <25>
PHO	#42,78# 10.6 (#78# and a second optimum at pH 8.2, oxidation of
	ethanol, pyrazole-sensitive enzyme <24>; #42# pyrazole-sensitive enzyme
	<25>) <24,25>
PHO	#43,46,56,60,84,91,92,111,118,126,132# 6 (#91,118# reduction of
	acetaldehyde <144,256>; #132# reduction of aldehyde <237>; #84#
	reduction reaction <226>; #126# aldehyde reduction <222>; #60# assay
	at, reverse reaction, ADH II <113>; #46# reduction of
	phenylacetaldehyde <149>; #92# reductive reaction <137>; #111# the
	optimal pH for reduction is at a pH of 6.0 <197>; #43# reductive
	reaction, all recombinant enzymes <232>)
	<113,137,144,147,149,197,222,226,232,237,256>
PHO	#45# 8.5-9.1 <153>
PHO	#45# 6.9-7.5 (#45# apparent optimal pH for the benzaldehyde reduction
	<154>) <154>
PHO	#5,77# -999 (#5# enzyme is strongly pH-dependent <110>; #77# pH
	dependence of the reaction mechanism and enzyme-substrate interaction,
	overview <130>) <110,130>
PHO	#5,8,9,20,72,121,131# 10.5 (#5# assay at <119>; #72# oxidation of
	ethanol <2>; #8# isoenzyme beta1,beta1 <20>; #8# isozyme ADH1B1, ADH4,
	assay at <119>; #121# oxidation of 1-hexanol <217>; #131# oxidation of
	2-pentanol <239>) <2,10,20,119,217,239,284>
PHO	#6,19,35# 9-10 (#19# oxidation of acetaldehyde <71>; #6# substrate:
	(S)-(-)-1-phenylethanol and 3 mM NAD+ or methyl benzoylformate + NADH
	<169>) <47,71,169>
PHO	#60,122# 5.5 (#122# assay at <219>; #60# assay at, reverse reaction,
	ADH I <113>) <113,219>
PHO	#67# 9.1 (#67# reduction of NAD+ <69>) <69>
PHO	#69# 8-8.4 (#69# reduction of aldehyde <84>) <84>
PHO	#69# 5.6-6.5 (#69# oxidation of ethanol <84>) <84>
PHO	#74# 9.9 (#74# and second optimum at pH 7.5 <64>) <64>
PHO	#78,81,122,123# 8.2 (#78# and a second optimum at pH 10.6, oxidation of
	ethanol, pyrazole-sensitive enzyme <24>; #122# oxidation reaction
	<219>; #123# oxidation of alcohols <219>) <24,83,219>
PHO	#8# 7.4 (#8# acetaldehyde reduction of isoenzyme beta2,beta2 <15>) <15>
PHO	#8# 7-7.5 (#8# and a second optimum at pH 10.0-10.5, ADH Indianapolis
	form 2 and 3 <22>) <22,211>
PHO	#8# 7.6 (#8# assay at, class II enzyme, reduction reaction <229>) <229>
PHO	#8# 8.5-8.8 (#8# ethanol oxidation, isoenzyme beta2,beta2, beta2,beta1,
	alpha,beta2 and beta2gamma1 <15>) <15>
PHO	#8# 10-10.5 (#8# and a second optimum at pH 10.0-10.5, ADH Indianapolis
	form 2 and 3 <22>) <22>
PHO	#8,10,51,88,121,136,137,138# 7 (#8# isoenzyme beta3,beta3 <20>; #8# ADH
	Indianapolis form 1 <22>; #121# reduction of benzaldehyde <217>; #10#
	free enzyme, at 25°C <196>) <20,22,82,132,196,217,252>
PHO	#8,12# 10.8 (#12# and a second lower maximum at pH 7.5 <45>) <12,45>
PHO	#8,18,41,87,123,128,132# 10 (#128# assay at <230>; #41# enzyme form
	ADH-II, oxidation of ethanol <67,68>; #8# standard assay at <115>;
	#123# alcohol oxidation reaction <218>; #132# optimally active with
	1-butanol at pH 10.0 with 4 M KCl <237>)
	<67,68,75,96,115,118,218,230,237>
PHO	#8,28# 5.9 (#8# acetaldehyde reduction, isoenzyme beta1,beta1 <15>)
	<15,133>
PHO	#8,40# 7.3 (#8,40# assay at <116,117>) <116,117>
PHO	#8,46# 10.4 (#46# oxidation of 2-phenylethanol <149>) <14,149>
PHO	#9# 10.7 (#9# oxidation of ethanol, isoenzyme 2, 3 and 4 <49>) <49>
PHO	#9,68,78,132# 11 (#78# oxidation of ethanol, pyrazole-insensitive
	enzyme <24>; #68# ethanol oxidation, enzyme form ADH-2 and ADH-3 <60>;
	#9# oxidation of octanol <49>; #132# optimally active with ethanol and
	1-propanol at pH 11.0 with 3 M KCl <237>) <24,49,60,237>
PHO	#91# 6.7-7 (#91# oxidation of ethanol <144>) <144>
PHO	#99# 7.7-8.6 (#99# reaction with ethanol + NAD+ <171>) <171>
PHO	#99# 6.7-7.3 (#99# reaction with acetaldehyde + NADH <171>) <171>

PH_RANGE
PHR	#10# 5-9 <196>
PHR	#10# 8.2-9.5 (#10# pH 8.2: about 10% of maximal activity, pH 9.5: about
	40% of maximal activity <87>) <87>
PHR	#10,113,114# 6-9 <122,215>
PHR	#110# 2-8 <213>
PHR	#121# 5.5-7.5 (#121# pH 5.5: about 35% of maximal activity, pH 7.5:
	about 55% of maximal activity, reduction of benzaldehyde <217>) <217>
PHR	#121# 7.5-10.8 (#121# pH 7.5: about 35% of maximal activity, pH 10.8:
	about 50% of maximal activity, oxidation of 1-hexanol <217>) <217>
PHR	#122# 6.7-8.5 (#122# pH 6.7: about 40% of maximal activity, pH 8.5:
	about 85% of maximal activity, oxidation reaction <219>) <219>
PHR	#122# 4.9-5.8 (#122# pH 4.9: about 25% of maximal activity, pH 5.8:
	about 40% of maximal activity, reduction reaction <219>) <219>
PHR	#127# 5.5-9 (#127# reduction reaction activity range, profile overview
	<225>) <225>
PHR	#127# 4-8.5 (#127# oxidation reaction activity range, profile overview
	<225>) <225>
PHR	#131# 7-9.6 (#131# pH 7.0: about 70% of maximal activity, pH 9.6: about
	50% of maximal activity, reduction of 2-pentanone <239>) <239>
PHR	#131# 9.6-11.5 (#131# pH 9.5: about 40% of maximal activity, pH 11.5:
	about 30% of maximal activity, oxidation of 2-pentanol <239>) <239>
PHR	#149# 6 (#149# 50% of maximum activity for reduction of aldehydes
	<243>) <243>
PHR	#20# 8.5 (#20# more than 50% of maximum activity <284>) <284>
PHR	#24,40# 6-10 <106,111>
PHR	#42# 9-12 (#42# pH 9.0: about 25% of maximal activity, pH 12.0: about
	80% of maximal activity, pyrazole-sensitive enzyme <25>) <25>
PHR	#42# 10-11 (#42# pH 10.0: about 50% of maximal activity, pH 11.0: about
	75% of maximal activity, pyrazole-insensitive enzyme <25>) <25>
PHR	#45# 8.8-9.6 <163>
PHR	#46# 5-8 (#46# pH 5.0: about 50% of maximal activity, pH 8.0: about 40%
	of maximal activity, reduction of phenylacetaldehyde <149>) <149>
PHR	#50# 5.5 (#50# complete inactivation <279>) <279>
PHR	#56# 4-8 (#56# pH 4.0: about 35% of maximal activity, pH 8.0: about 70%
	of maximal activity <147>) <147>
PHR	#68# 9.5-11.5 (#68# pH 9.5: about 40% of maximal activity, pH 11.5:
	about 85% of maximal activity, ethanol oxidation enzyme form ADH-3
	<60>) <60>
PHR	#69# 5.2-6.8 (#69# pH 5.2: about 35% of maximal activity, pH 6.8: about
	55% of maximal activity, oxidation of ethanol <84>) <84>
PHR	#69# 7.2-9.2 (#69# pH 7.2: about 50% of maximal activity, pH 9.2: about
	60% of maximal activity <84>) <84>
PHR	#8# 8-10.5 (#8# pH 8.0: about 40% of maximal activity, pH 10.5: about
	85% of maximal activity <96>) <96>
PHR	#8,30,46# 8-12 (#8# about 30% of maximal activity at pH 8.0 and at pH
	12.0 <14>; #46# pH 8.0: about 50% of maximal activity, pH 12.0: about
	50% of maximal activity, oxidation of 2-phenylethanol <149>; #30# pH
	8.0: about 70% of maximal activity, pH 12: about 60% of maximal
	activity <181>) <14,149,181>
PHR	#96# 4-7.5 (#96# pH 4.0: about 80% of maximal activity, pH 7.5: about
	60% of maximal activity <168>) <168>
PHR	#98# 7-8 (#98# pH 7: 41% of maximal activity, pH 8: 59% of maximal
	activity <173>) <173>

SPECIFIC_ACTIVITY
SA	#1,12,14,18,40,60,67,80,83,89# -999.0 (#60# activity of the 2 isozmyes
	with various substrates, overview <113>; #83# wild-type and mutant
	enzymes <125>) <35,44,46,69,75,77,81,105,113,125>
SA	#10# 0.47 (#10# substrate furfural, pH 7.0, 30°C <285>) <285>
SA	#10# 6.5 (#10# substrate glycolaldehyde, pH 7.0, 30°C <285>) <285>
SA	#10# 0.44 (#10# substrate formaldehyde, pH 7.0, 30°C <285>) <285>
SA	#10# 5.18 (#10# pH 6.7, 30°C, mutant enzyme S109P/L116S/Y294C <193>)
	<193>
SA	#100# 31.0 <185>
SA	#104# 0.5 (#104# purified mutant enzyme W95L, using benzyl alcohol as
	substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C <207>) <207>
SA	#104# 18.6 (#104# purified mutant enzyme W95L/N249Y, using benzyl
	alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
	<207>) <207>
SA	#106# 2.6 (#106# in Tris-HCl buffer (pH 7.6), 5 mM dithiothreitol, 0.2
	mM NADH, and 10 mM acetaldehyde at 65°C <195>) <195>
SA	#110# 17.6 (#110# crude extract Ta1316 ADH with ethanol as a substrate,
	at pH 5.0 and 75°C <213>) <213>
SA	#110# 628.7 (#110# purified Ta1316 ADH with ethanol as a substrate, at
	pH 5.0 and 75°C <213>) <213>
SA	#111# 20.6 (#111# after 1.4fold purifictaion <197>) <197>
SA	#111# 15.0 (#111# crude enzyme, after heat treatment at 75°C for 20
	min <197>) <197>
SA	#113# 447.0 (#113# substrate ethanol, pH 8.0, 60°C <215>) <215>
SA	#12# 2.69 <45>
SA	#122# 6.6 (#122# pH 5.5, 65°C <219>) <219>
SA	#127# 27.6 (#127# purified native enzyme, pH 6.5, 30°C <225>) <225>
SA	#142# 108.0 (#142# substrate butan-2,3-diol, maximal specific activity
	detected in oxidation reaction, 70°C, pH 8.8 <138>) <138>
SA	#142# 2.0 (#142# substrate diacetyl-acetoin, maximal specific activity
	detected in reduction reaction, 70°C, pH 6.1 <138>) <138>
SA	#143# 0.05 (#143# wild-type, cosubstrate NADPH, pH 7.0, 55°C <259>)
	<259>
SA	#143# 7.68 (#143# wild-type, cosubstrate NADH, pH 7.0, 55°C <259>)
	<259>
SA	#143# 0.07 (#143# gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0,
	55°C <259>) <259>
SA	#146# 0.25 (#146# gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0,
	55°C <259>) <259>
SA	#146# 0.68 (#146# wild-type, cosubstrate NADPH, pH 7.0, 55°C <259>)
	<259>
SA	#146# 1.52 (#146# wild-type, cosubstrate NADH, pH 7.0, 55°C <259>)
	<259>
SA	#152# 79.6 (#152# substrate butan-1-ol, pH 6.5, 60°C <272>) <272>
SA	#18# 70.0 (#18# wild-type enzyme Adh1-1S <97>) <97>
SA	#18# 65.0 (#18# mutant enzyme Adh1-1S1108 <97>) <97>
SA	#21# 17.17 <72>
SA	#23# 0.092 (#23# partially purified enzyme <128>) <128>
SA	#25# 3.12 <188>
SA	#35# 2.1 (#35# isoenzyme AA-ADH <95>) <95>
SA	#35# 4.0 <47>
SA	#35,57# 2.5 (#35# isoenzyme BB-ADH <95>) <95,147>
SA	#37# 79.1 <85>
SA	#4# 55.0 <65>
SA	#40# 2.0 <27>
SA	#40# 3.2 (#40# reduction of 3-oxo-5beta-androstan-17beta-ol <42>) <42>
SA	#40,104# 4.2 (#40# reduction of cyclohexanone <42>; #104# purified wild
	type enzyme, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH
	buffer (pH 10.5), at 65°C <207>) <42,207>
SA	#41# 93.0 (#41# enzyme form ADHI <68>) <68>
SA	#41# 470.0 (#41# enzyme form ADHII <68>) <68>
SA	#45# 3.92 <66>
SA	#45# 4.5 (#45# wild type recombinant enzyme, after 450fold
	purification, at 65°C <165>) <165>
SA	#45# 5.2 (#45# mutant recombinant enzyme E97C, after 260fold
	purification, at 65°C <165>) <165>
SA	#45# 5.3 <70>
SA	#45# 10.1 (#45# after 12.9fold purification, at pH 10.0 <159>) <159>
SA	#45# 4.1 (#45# wild type enzyme, at 65°C <154>) <154>
SA	#45# 0.02 (#45# mutant recombinant enzyme E97C, from crude extract, at
	65°C <165>) <165>
SA	#45# 4.03 (#45# recombinant wild type enzyme, after 6fold purification,
	at 65°C <163>) <163>
SA	#45# 0.78 (#45# crude extract, at pH 10.0 <159>) <159>
SA	#45# 0.64 (#45# wild type enzyme, crude extract, at 65°C <163>) <163>
SA	#45# 26.1 (#45# mutant enzyme N249Y, at 65°C <154>) <154>
SA	#45,146# 0.01 (#45# wild type recombinant enzyme, from crude extract,
	at 65°C <165>; #146# gene AdhE deletion mutant, cosubstrate NADH, pH
	7.0, 55°C <259>) <165,259>
SA	#45,91# 43.0 (#45# mutant enzyme N249Y, after 6fold purification, at
	65°C <163>) <144,163>
SA	#47# 0.3 (#47# substrates 1,3-propanediol and NAD+, pH 9.0, 60°C,
	recombinant enzyme, with NiCl2 addition <223>) <223>
SA	#47# 1.1 (#47# substrates ethanol and NAD+, pH 9.0, 60°C, recombinant
	enzyme <223>) <223>
SA	#5# 1.36 (#5# isoenzyme A2 <48>) <48>
SA	#5# 64.0 (#5# isoenzyme C2 <48>) <48>
SA	#5# 8.08 (#5# isoenzyme B2 <48>) <48>
SA	#50# 1.7 (#50# cofactor NAD+, pH 7.0, 30°C <279>) <279>
SA	#50,93,143# 0.03 (#93# crude extract, using benzylalcohol as substrate,
	at 65°C <162>; #143# gene AdhE deletion mutant, cosubstrate NADH, pH
	7.0, 55°C <259>; #50# cofactor NADP+, pH 7.0, 30°C <279>)
	<162,259,279>
SA	#51# 49.3 <82>
SA	#54# 31.8 <99>
SA	#56# 2.3 <147>
SA	#6# 151.1 <169>
SA	#60# 361.0 (#60# purified ADH II <113>) <113>
SA	#60# 597.0 (#60# purified ADH I <113>) <113>
SA	#66# 55900.0 <78>
SA	#69# 196.3 <84>
SA	#8# 3.3 <12>
SA	#8# 0.6 <16>
SA	#8# 0.65 <21>
SA	#8# 1.47 <14>
SA	#8,9# 1.3 (#9# ADH-3 <49>) <18,49>
SA	#84# 4.75 (#84# purified recombinant enzyme, pH 6.5, 50°C <226>) <226>
SA	#87# 1.28 (#87# purified enzyme <118>) <118>
SA	#9# 0.1 (#9# isoenzyme 4 <49>) <49>
SA	#9# 32.5 (#9# ADH-1 <49>) <49>
SA	#9# 0.12 (#9# isoenzyme 1 <49>) <49>
SA	#9,121# 1.14 (#9# ADH-2 <49>; #121# pH 10.5, 50°C <217>) <49,217>
SA	#9,47# 0.2 (#9# isoenzyme 3 <49>; #47# substrates 1,3-propanediol and
	NAD+, pH 9.0, 60°C, recombinant enzyme <223>; #47# substrates
	acetaldehyde and NADH, pH 8.0, 60°C, recombinant enzyme <223>) <49,223>
SA	#9,79# 0.62 (#9# isoenzyme 2 <49>) <49,52>
SA	#92# 10.3 <137>
SA	#93# 0.75 (#93# purified enzyme, using benzylalcohol as substrate, at
	80°C <162>) <162>
SA	#93# 0.18 (#93# after 5.67fold purification, using benzylalcohol as
	substrate, at 65°C <162>) <162>
SA	#94# 0.22 (#94# crude extract, at pH 10.0 <159>) <159>
SA	#94# 2.88 (#94# after 12.9fold purification, at pH 10.0 <159>) <159>
SA	#98# 0.225 <173>

TEMPERATURE_OPTIMUM
TO	#10# 25-30 (#10# assay at <120>) <120>
TO	#10# 45-50 <3>
TO	#10,26,50,54# 40 (#26# assay at <129>; #10# Cu-ADH <122>; #10# enzyme
	covalently immobilized to magnetic Fe3O4 nanoparticles via
	glutaraldehyde <182>) <99,122,129,182,279>
TO	#10,43,96# 35 (#10# immobilized enzyme <196>; #10# Zn-ADH and Co-ADH
	<122>; #43# reductive reaction, recombinant enzymes expressed from
	Saccharomyces cerevisiae and Hansenula polymorpha <232>; #43#
	recombinant enzyme expressed in Hansenula polymorpha <232>; #43#
	recombinant enzyme expressed in Saccharomyces cerevisiae <232>; #10#
	reduction of glycolaldehyde, furfural, butyraldehyde, and
	propionaldehyde <285>) <122,168,196,232,285>
TO	#10,69,100,127# 30 (#10# soluble enzyme <182>; #127# assay at <225>;
	#100# reduction of N-benzyl-3-pyrrolidinone <185>; #10# approximately
	30°C <205>; #10# reduction of formaldehyde <285>)
	<84,144,182,185,205,225,285>
TO	#104,132# 80 (#104# assay at <235>) <235,237>
TO	#110,122,123# 75 <213,219>
TO	#113,114,156# 60 (#156# enzyme expressed in Pyrococcus furiosus <281>)
	<215,281>
TO	#123# 78 (#123# the reaction rate increases up to 78°C and then
	decreases rapidly due to thermal inactivation <218>) <218>
TO	#13,30,40,51,84,87,91,128# 70 (#128# assay at <230>; #51# above <82>;
	#13# recombinant enzyme <126>; #40# approximately 70°C <205>)
	<82,118,126,144,181,205,226,230>
TO	#131# 95 (#131# catalytic activity increased up to 95°C <239>) <239>
TO	#136,138# 45 <252>
TO	#142# 100 <138>
TO	#149# 90 <243>
TO	#15,28# 33 <133,134>
TO	#23,126# 22 (#23,126# assay at room temperature <128,222>) <128,222>
TO	#25,137,150# 55 (#150# oxidation of crotyl aclohol <244>) <188,244,252>
TO	#37# 50-55 <85>
TO	#40# 37 (#40# assay at <117>) <117>
TO	#43# 30-50 <114>
TO	#43# 39 (#43# reductive reaction, recombinant enzyme expressed from
	Arxula adeninivorans <232>; #43# recombinant enzyme expressed in Arxula
	adeninivorans <232>) <232>
TO	#47# 50-60 <223>
TO	#5,8,10,24,39,60# 25 (#5,8,10# assay at <107,115,119,121,124,229>; #60#
	assay at, forward and reverse reaction <113>; #10# free enzyme, at
	25°C <196>) <106,107,113,115,119,121,124,131,196,229>
TO	#6# 73 <169>
TO	#70,121# 85 (#70# approximately 85°C <205>) <205,217>
TO	#70,122,123,150# 65 (#70,122,123# assay at <121,218,219>; #150#
	reduction of crotonaldehyde <244>) <121,218,219,244>
TO	#8,40# 30-37 (#8,40# assay at <116>) <116>
TO	#92,99,121,135# 50 (#121# assay at <217>; #99# reaction with ethanol +
	NAD+ <171>) <137,171,217,252>
TO	#98# 83 <173>

TEMPERATURE_RANGE
TR	#10# 15-50 <122,196>
TR	#10# 20-85 (#10# 20°C: about 65% of maximal activity, 85°C: about 90%
	of maximal activity <144>) <144>
TR	#110# 25-90 <213>
TR	#121# 70-95 (#121# 70°C: about 65% of maximal activity, 95°C: about
	80% of maximal activity <217>) <217>
TR	#122,123# 65-85 (#122# 65°C: about 40% of maximal activity, 85°C:
	about 35% of maximal activity <219>; #123# 65°C: about 60% of maximal
	activity, 85°C: about 70% of maximal activity <218>) <218,219>
TR	#127# 10-75 (#127# activity range, profile overview <225>) <225>
TR	#132# 60-90 (#132# 60°C: 75% of maximal activity, 90°C: 75% of
	maximal activity <237>) <237>
TR	#25# 30-65 (#25# 30°C: 36% of maximal activity, 65°C: 24% of maximal
	activity <188>) <188>
TR	#27# 10-45 (#27# activity increases from 10°C to 45°C <74>) <74>
TR	#30# 50-80 (#30# 50°C: 45% of maximal activity, 80°C: about 60% of
	maximal activity <181>) <181>
TR	#45# 45-95 (#45# continous increase in activity from 40°C to 95°C
	<66>) <66>
TR	#46# 60 <149>
TR	#47# 10-80 (#47# more than 40% of activity between 40°C and 70°C with
	all substrates. The enzyme is not capable of reducing acetaldehyde at
	80°C, while remaining activity for alcohol oxidation, temperature
	optimum lies between 50°C to 60°C <223>) <223>
TR	#69# 10-60 (#69# 10°C: about 65% of maximal activity, 50°C: about 40%
	of maximal activity <84>) <84>
TR	#87# 30-85 (#87# maximal activity at 70°C, 60% of maximal activity at
	85°C <118>) <118>
TR	#88# 33-35 <132>
TR	#91# 0-60 (#91# 0°C: about 70% of maximal activity, about 45% of
	maximal activity <144>) <144>
TR	#92# 20-70 (#92# 20°C: 23% of maximal activity, 70°C: 40% of maximal
	activity <137>) <137>
TR	#96,100# 20-50 (#96# 20°C: about 80% of maximal activity, 50°C: about
	55% of maximal activity <168>; #100# 20°C: about 80% of maximal
	activity, 50°C: about 60% of maximal activity, reduction of
	N-benzyl-3-pyrrolidinone <185>) <168,185>
TR	#98# 75-90 (#98# 75°C: about 45% of maximal activity, 90°C: about 45%
	of maximal activity <173>) <173>

COFACTOR
CF	#1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,21,22,23,26,27,31,32
	33,35,37,38,40,41,42,43,44,45,46,47,49,50,51,52,54,58,59,60,62,63,65,66
	67,68,69,70,71,72,73,74,75,76,77,78,79,80,81,82,83,84,85,86,87,89,90,91
	92,93,94,95,97,104,105,106,107,108,109,110,111,112,113,114,118,121,122
	123,124,125,126,127,128,129,132,136,137,138,139,141,142,149,152# NAD+
	(#13,23,43,60,109,111# dependent on <113,114,126,128,197,210>; #45,94#
	dependent <153,154,159>; #40# kinetics of coenzyme binding in the
	pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced conversion <62>;
	#40# NAD+ acts as an activator which induces an active form of the
	enzyme <34>; #40# preferred substrate <42>; #83# activity with mutants
	G223D/T224I and G223D/T224I/H225N <125>; #10# cofactor binding mode
	<120>; #13# dependent on, cofactor binding mechanism and conformation
	from crystal structure analysis <112>; #86# the monomer consists of a
	catalytic and a cofactor-binding domain, the cofactor is bound between
	2 domains in a cleft <127>; #7,26,33,49,65# strongly preferred as
	cofactor <135>; #91# specific for NAD+, no activity with NADP+, pro-R
	stereospecificity for hydrogen transfer <144>; #97# ADH1 preferrs NAD+
	205fold better than NADP+ as cofactor <172>; #15# ADH3 does not react
	with NADP+ <172>; #142# preferred over NADP+ <138>; #6# strict
	requirement for NAD(H) as the coenzyme. Critical role of the D37
	residue in discriminating NAD(H) from NADP(H) <169>; #110# shows NAD+
	as the preferred co-factor over NADP+ <213>; #40# the binding of NAD+
	is kinetically limited by a unimolecular isomerization (corresponding
	to the conformational change) that is controlled by deprotonation of
	the catalytic zinc-water to produce a negatively-charged
	zinc-hydroxide, which can attract the positively-charged nicotinamide
	ring <198>; #113# NAD+ is prefered over NADP+ <215>; #114# NADP+ is
	prefered over NAD+ <215>; #123# strict requirement for NAD(H) as the
	coenzyme, no activity with NADP+. The specificity constant value is
	6fold higher for NADH than NAD+ <218>; #122# the enzyme transfers the
	deuteride to the Si-face of NAD+ <219>; #47# Adh3 is strictly dependent
	on NAD+/NADH, and shows no activity with NADP+/NADPH as cofactor <223>;
	#132# exclusively NAD+ dependent <237>; #50# 57fold preferred over
	NADP+ <279>)
	<1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26
	27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50
	51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74
	75,76,77,78,79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98
	99,100,101,102,103,105,110,111,112,113,114,115,116,118,120,121,124,125
	126,127,128,129,130,135,136,137,138,139,141,143,144,146,148,149,152,153
	154,156,157,158,159,161,162,163,164,165,169,172,180,194,195,196,197,198
	200,201,202,203,204,205,206,207,208,209,210,211,212,213,214,215,217,218
	219,220,221,222,223,225,226,227,229,230,231,232,233,234,237,243,252,254
	256,257,260,269,272,279>
CF	#1,2,3,4,5,6,8,9,10,11,12,13,14,15,16,17,18,19,21,22,23,26,27,28,31,32
	35,37,38,39,40,41,42,43,44,45,46,47,51,52,53,54,58,60,62,63,66,67,68,69
	71,72,73,74,75,76,77,78,79,80,81,82,83,84,87,88,89,92,114,118,121,122
	123,124,125,126,127,135,136,137,140,143,146,148,152,155,156# NADH
	(#127# required <225>; #43,60# dependent on <113,114>; #45# dependent
	<155>; #40# kinetics of coenzyme binding in the pH range 10-12 <26>;
	#40# preferred coenzyme <42>; #83# activity with mutants G223D/T224I
	and G223D/T224I/H225N <125>; #10# cofactor binding mode <120>; #123#
	strictly required <219>; #6# strict requirement for NAD(H) as the
	coenzyme. Critical role of the D37 residue in discriminating NAD(H)
	from NADP(H) <169>; #123# strict requirement for NAD(H) as the
	coenzyme, no activity with NADPH. The specificity constant value is
	6fold higher for NADH than NAD+ <218>; #122# the specificity constant
	value is 21-fold higher for NADH than NAD+. No activity with NADP(H)
	<219>; #47# Adh3 is strictly dependent on NAD+/NADH, and shows no
	activity with NADP+/NADPH as cofactor <223>; #6# the enzyme transfers
	the pro-S hydrogen of [4R-(2)H]NADH and exhibits Prelog specificity
	<269>)
	<1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26
	27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50
	51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74
	75,76,77,78,79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98
	99,100,101,102,105,110,113,114,118,120,123,124,125,129,131,132,133,134
	137,140,149,151,155,157,158,161,163,169,200,215,217,218,219,222,223,225
	226,231,232,233,234,241,246,252,253,256,259,265,269,272,281,285>
CF	#10,12,14,35,40,50,54,67,70,83,113,114,142,149# NADP+ (#12,14,35,67# no
	activity as coenzyme <45,47,69,81>; #40# also utilized as coenzyme by
	the SS isoenzyme <28>; #54# at 1.5% of the activity with NAD+ <99>;
	#142# 14% of the activity with NAD+ <138>; #83# specific for, residues
	Gly223, Thr224, His225, Leu200, and Lys228 are involved in cofactor
	binding pocket formation <125>; #113# NAD+ is prefered over NADP+
	<215>; #114# NADP+ is prefered over NAD+ <215>; #50# NAD+ is 57fold
	preferred over NADP+ <279>)
	<28,45,47,69,81,99,103,121,125,138,215,243,279>
CF	#10,40,46,77,84,150,153# more (#10# no activity with NADPH <285>; #10#
	kinetic study on the binding of monomeric and polymeric derivatives of
	NAD+ <88>; #40# kinetics of native and modified enzyme with coenzyme
	analogues <54>; #77# crystallographic study of the coenzyme binding
	mode <38>; #46# NADP+ shows less than 0.1% of the activity with NAD+
	<149>; #84# the enzyme prefers NAD(H) over NADP(H) as a cofactor <226>;
	#150# no activity with NAD(H) <244>; #153# in presence of propan-2-ol
	at 10% v/v, reduction of fluorinated ketones is catalyzed without
	addition of NADH <280>) <38,54,88,149,226,244,280,285>
CF	#14,40,53,54,83,92,114,143,146,150# NADPH (#54# at 1.6% of the activity
	with NADH <99>; #14# no activity as coenzyme <81>; #40# also utilized
	as coenzyme by the SS isoenzyme <28>; #83# specific for, residues
	Gly223, Thr224, His225, Leu200, and Lys228 are involved in cofactor
	binding pocket formation <125>; #53# about 20% of the activity with
	NADH <151>; #92# weak activity <137>; #150# enzyme strictly requires
	NADP(H) as a coenzyme <244>) <28,81,99,125,137,151,215,244,259,265>
CF	#40# 3-benzoylpyridine-adenine dinucleotide (#40# can be used as
	coenzyme <33>) <33>
CF	#40# acycloNAD+ (#40# NAD+-analogue, where the nicotinamide ribosyl
	moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl
	moiety. The chemical properties are comparable to those of beta-NAD+
	with a redox potential of -324 mV and a 341 nm lambdamax for the
	reduced form. The stereochemistry of the hydride transfer in the
	oxidation of n-butanol is identical to that for the reaction with
	beta-NAD+. There is no detectable reduction of acycloNAD+ by secondary
	alcohols although these alcohols serve as competitive inhibitors.
	AcycloNAD+ converts horse liver ADH from a broad spectrum alcohol
	dehydrogenase, capable of utilizing either primary or secondary
	alcohols, into an exclusively primary alcohol dehydrogenase <275>) <275>

ACTIVATING_COMPOUND
AC	#10# Glutaraldehyde (#10# treating with 0.5% glutaraldehyde solution,
	the activity of the immobilized enzyme is at maximum <196>) <196>
AC	#111# Urea (#111# 130% relative activity at 1 M <197>) <197>
AC	#111# Triton X-100 (#111# 201% relative activity at 10% (v/v) <197>)
	<197>
AC	#122# 2-propanol (#122# 120–125% activation after incubation for 25 h
	in the presence of 17% 2-propanol. High concentration (30%) result in
	enzyme inactivation to 5–30% of the initial values following 5 h
	incubation at 50°C <219>) <219>
AC	#122# 1,4-dioxane (#122# significant increases in enzyme activity
	occurs after 25 h incubation at a concentration of 30% <219>) <219>
AC	#122# n-hexane (#122# significant increases in enzyme activity occurs
	after 25 h incubation at a concentration of 30% <219>) <219>
AC	#122# n-heptane (#122# significant increases in enzyme activity occurs
	after 25 h incubation at a concentration of 30% <219>) <219>
AC	#122# TBME (#122# significant increases in enzyme activity occurs after
	25 h incubation at a concentration of 30% <219>) <219>
AC	#123# 2-mercaptoethanol (#123# 5 mM, 112% of initial activity <219>)
	<219>
AC	#150# dithiothreitol (#150# 1 mM, 123% of initial activity <244>) <244>
AC	#25# iodoacetate (#25# 1 mM, 1.1fold activation <188>) <188>
AC	#40# Acetylsalicylate (#40# enhances activity <143>) <143>
AC	#40# tert-butyl hydroperoxide (#40# stimulation up to 100 mM <86>) <86>
AC	#40,128# more (#40# isonicotinimidylation and methylation increases
	activity <35>; #128# without heat treatment the AdhC enzyme shows no
	detectable activity, but after 10 min at higher temperatures the
	activity is revealed. The highest activity is measured after 10 min at
	100°C <230>) <35,230>
AC	#45# iodoacetamide (#45# 1 mM activates up to 25fold <163>) <163>
AC	#5# tert-butanol (#5# activates ADH3 <141>) <141>
AC	#5# butyramide (#5# activates ADH3 <141>) <141>
AC	#5# Valeramide (#5# activates ADH3 <141>) <141>
AC	#5# capronamide (#5# activates ADH3 <141>) <141>
AC	#5# S-nitrosoglutathione (#5# ADH3-mediated alcohol oxidation is
	promoted in the presence of S-nitrosoglutathione <200>) <200>
AC	#6,51,113,150# EDTA (#51# enhances activity <82>; #6# 10 mM, 1.65fold
	activation <169>; #150# 1 mM, 110% of initial activity <244>; #113# 1
	mM, 105% of initial activity <215>) <82,169,215,244>
AC	#86,122# acetonitrile (#122# 120–125% activation after incubation for
	25 h in the presence of 17% acetonitrile. High concentration (30%)
	result in enzyme inactivation to 5–30% of the initial values
	following 5 h incubation at 50°C <219>; #86# the enzyme is activated
	by water-miscible organic solvents <238>) <219,238>

INHIBITORS
IN	#10# NaCN <94>
IN	#10# acetamide <94>
IN	#10# butyramide <91>
IN	#10# furfural <282>
IN	#10# mithramycin <209>
IN	#10# 2-fluoroethanol <94>
IN	#10# chromomycin A3 <209>
IN	#10# 5-hydroxymethylfurfural <282>
IN	#10# heptafluorobutanol <91>
IN	#10# tert-butyl hydroperoxide (#10# irreversible, inactivation is
	associated with -SH group oxidation <86>) <86>
IN	#10# Glutaraldehyde (#10# 71% relative activity in the presence of 10
	mM glutaraldehyde <196>) <196>
IN	#10# starch (#10# enzyme activity decreases to half of its original
	activity at 10 mg/ml of starch. The thiol groups of alcohol
	dehydrogenase are involved in binding <278>) <278>
IN	#10# Pectin (#10# enzyme activity decreases to half of its original
	activity at 2 mg/ml of pectin. The thiol groups of alcohol
	dehydrogenase are involved in binding <278>) <278>
IN	#10# D-glucose (#10# enzyme activity decreases to half of its original
	activity at 4 mg/ml of D-glucose. The thiol groups of alcohol
	dehydrogenase are involved in binding <278>) <278>
IN	#10,11,17,18,19,22,40,44,45,49,63,118,122,127# more (#40# design of
	inhibitors <31>; #11,17,18,19,22,44,63# inactivator from rice seedlings
	<80>; #10# use of competitive dead-end inhibitors to determine the
	chemical mechanism of action of yeast alcohol dehydrogenase <94>; #40#
	thiols and dithiols have their main effect, at the enzyme-NAD+-thiol
	complex level, by competition with alcohol for the catalytic zinc <98>;
	#49# no inhibition by 4-methylpyrazole <135>; #45# not affected by Cu2+
	<163>; #122# the chlorides of Li+, Na+, K+, Ca2+, Mg2+, and Mn2+ do not
	affect the activity of the enzyme, whereas the sulfate of heavy metal
	ions such as Fe2+, Co2+, and Cu2+ cause a slight inactivation <219>;
	#127# no inhibition by 4-chloromercuribenzoate at 0.1 mM and by CuSO4
	at 1 mM, poor effects by EDTA, 1,20-phenanthroline, 2-mercaptoethanol,
	and DTT <225>; #118# no inhibitory: Triton X-100 at 1%, guanidinium
	hydrochloride at 0.2 M <256>) <31,80,94,98,135,163,219,225,256>
IN	#10,37,87,89# acetaldehyde (#37# linear noncompetitive inhibition <85>;
	#87# strong product inhibition <118>; #89# product inhibition, 50%
	inhibition at 16 mM <105>) <85,105,118,282>
IN	#10,40# H2O2 (#40# inactivation is caused by oxidation of its
	functional Cys residues, coenzyme protects from inactivation <40>)
	<40,189>
IN	#10,77,101# 2,2,2-Trifluoroethanol (#77# competitive towards ethanol
	<61>; #101# 95 mM, 74% inhibition <174>) <61,94,174>
IN	#10,91,98,111# SDS (#91# 1 mM, 91% inhibition <144>; #98# 10% (w/v),
	95% inhibition <173>; #10# in the presence of the surfactant the
	initial reaction rates are consistently lower than in pure buffer at
	all the surfactant concentrations considered (0.5-50 mM). This effect
	is mainly due to an increase in the dissociation constant of beta-NAD+
	which reaches its maximum value (7.1 mM) at the critical micelle
	concentration. Above the critical micelle concentration the effect of
	the surfactant is mainly due to an increase in the Michaels constants
	of the alcohol, with values of 41 mM for 15 mM SDS and 50 mM for 50 mM
	SDS <192>; #111# 0.4% relative activity at 10% (v/v) <197>)
	<144,173,192,197>
IN	#100,122,127# ZnSO4 (#100# 1 mM, complete inhibition <185>; #127# 26%
	inhibition at 1 mM <225>; #122# 1 mM, 9% inhibition <219>) <185,219,225>
IN	#100,127# CoCl2 (#100# 1 mM, 37% inhibition <185>; #127# 15% inhibition
	at 1 mM <225>) <185,225>
IN	#101# Antimycin (#101# 0.0017 mM, 95% inhibition <174>) <174>
IN	#113,114# sodium dodecylsulfate (#113# 1 mM, 3% residual activity
	<215>; #114# 1 mM, no residual activity <215>) <215>
IN	#118# Butyraldehyde <246>
IN	#12,150# Ag+ (#150# 1 mM, no residual activity <244>) <45,244>
IN	#12,18,30,47,51,54,56,57,111,113,114,123,150# Zn2+ (#51# 0.1 mM, 20%
	decrease of activity <82>; #47# complete inhibition <223>; #57# 5 mM,
	17% loss of activity <147>; #56# 5 mM, 29% loss of activity <147>;
	#111# 91% relative activity at 10 mM <197>; #114# 1 mM, 14.1% residual
	activity <215>; #113# 1 mM, 30.5% residual activity <215>; #150# 1 mM,
	0.5% residual activity <244>; #123# 1 mM, 91% of initial activity
	<219>) <45,76,82,99,147,181,197,215,219,223,244>
IN	#12,18,37,41,46,54,91,100# PCMB (#18# no effect <76>; #100# 0.1 mM,
	complete inhibition <185>; #46,91# 1 mM, complete inhibition <144,149>)
	<45,68,75,76,85,99,144,149,185>
IN	#12,18,54,91,127# NEM (#91# 1 mM, complete inhibition <144>; #127# 17%
	inhibition at 1 mM <225>) <45,75,99,144,225>
IN	#12,37,91,100# iodoacetic acid (#100# 1 mM, 10% inhibition <185>; #91#
	1 mM, 96% inhibition <144>) <45,85,144,185>
IN	#12,40,66# glutathione (#40# competitive <98>) <45,78,98>
IN	#12,54# 2,2'-dipyridyl <45,99>
IN	#122# NaCl (#122# 1 mM, 12% inhibition <219>) <219>
IN	#122# CoSO4 (#122# 1 mM, 11% inhibition <219>) <219>
IN	#122# Hg(CH3COO)2 (#122# 1 mM, 37% inhibition <219>) <219>
IN	#122# 2-propanol (#122# 120–125% activation after incubation for 25 h
	in the presence of 17% 2-propanol. High concentration (30%) result in
	enzyme inactivation to 5–30% of the initial values following 5 h
	incubation at 50°C <219>) <219>
IN	#122# acetonitrile (#122# 120–125% activation after incubation for 25
	h in the presence of 17% acetonitrile. High concentration (30%) result
	in enzyme inactivation to 5–30% of the initial values following 5 h
	incubation at 50°C <219>) <219>
IN	#122# 1,4-dioxane (#122# 30%, 5–30% inactivation of the initial
	values following 5 h incubation at 50°C <219>) <219>
IN	#122,127# iodoacetate (#122# 1 mM, 12% inhibition <219>; #127# 20%
	inhibition at 1 mM <225>) <219,225>
IN	#127# MnCl2 (#127# 24% inhibition at 1 mM <225>) <225>
IN	#127# MgSO4 (#127# 19% inhibition at 1 mM <225>) <225>
IN	#127# quercetin (#127# 22% inhibition at 0.01 mM <225>) <225>
IN	#13,77,87# imidazole (#87# weak inhibition <118>; #77# pure competitive
	inhibition towards ethanol and (R)-(+)-phenylethanol <61>) <61,118,126>
IN	#13,87# Pyridine <118,126>
IN	#18# p-hydroxymercuribenzoate <75>
IN	#18# PMSF <75>
IN	#18# B4O72- <76>
IN	#18,67# iodoacetamide <69,75,76>
IN	#23# cyclopropyl carbinol (#23# complete inhibition in vitro at 1820
	nM, anti-amoebic activity on trophozoites by growth inhibition of
	recombinant Escherichia coli cells <123>) <123>
IN	#23# cyclobutyl carbinol (#23# complete inhibition in vitro at 890 nM,
	anti-amoebic activity on trophozoites by growth inhibition of
	recombinant Escherichia coli cells <123>) <123>
IN	#25# 2,4-dinitrophenol (#25# 1 mM, complete inhibition <188>) <188>
IN	#25# N-ethylmaleimide (#25# 1 mM, 11% inhibition <188>) <188>
IN	#25,100,111# 2,2'-bipyridyl (#25# 1 mM, 11% inhibition <188>; #100# 1
	mM, 78% inhibition <185>; #111# 91% relative activity at 10 mM <197>)
	<185,188,197>
IN	#25,111# dithiothreitol (#25# 1 mM, 6% inhibition <188>; #111# 14%
	relative activity at 10 mM <197>) <188,197>
IN	#25,122# FeSO4 (#25# 1 mM, complete inhibition <188>; #122# 1 mM, 20%
	inhibition <219>) <188,219>
IN	#25,40,66# 2-mercaptoethanol (#40# competitive <98>; #25# 1 mM, 19%
	inhibition <188>) <78,98,188>
IN	#25,46# BaCl2 (#25# 1 mM, complete inhibition <188>; #46# 1 mM, 95%
	inhibition <149>) <149,188>
IN	#25,46,92# PbCl2 (#25# 1 mM, complete inhibition <188>; #46# 1 mM, 24%
	inhibition <149>; #92# 1 mM, 63% inhibition <137>) <137,149,188>
IN	#25,92# AgNO3 (#25# 1 mM, 37% inhibition <188>; #92# 0.1 mM, 66%
	inhibition <137>) <137,188>
IN	#3# pyridoxal 5'-phosphate (#3# inactivates by modifying its
	epsilon-amino group, NAD+ protects <4>) <4>
IN	#35# 12-hydroxydodecanoate <47>
IN	#35# testosterone (#35# inhibition of isoenzyme BB-ADH, no inhibition
	of isoenzyme AA-ADH and TT-ADH <95>) <95>
IN	#35# genistein (#35# inhibition of isoenzyme BB-ADH, no inhibition of
	isoenzyme AA-ADH and TT-ADH <95>) <95>
IN	#35# daidzein (#35# inhibition of isoenzyme BB-ADH, no inhibition of
	isoenzyme AA-ADH and TT-ADH <95>) <95>
IN	#35# Biochanin A (#35# inhibition of isoenzyme BB-ADH, no inhibition of
	isoenzyme AA-ADH and TT-ADH <95>) <95>
IN	#4,37,77# NADH (#4,77# competitive towards NAD+ <61,63>; #37# linear
	competitive inhibition <85>) <43,61,63,85>
IN	#4,98# acetone (#4# product inhibition <43>; #98# 50% (v/v), 82% loss
	of activity <173>) <43,173>
IN	#40# dimethyl sulfoxide <175>
IN	#40# diethyldithiocarbamate (#40# competitive <98>) <98>
IN	#40# captopril (#40# competitive <98>) <98>
IN	#40# coenzyme A (#40# competitive <98>) <98>
IN	#40# Cys (#40# competitive <98>) <98>
IN	#40# cysteamine (#40# competitive <98>) <98>
IN	#40# Thiourea (#40# competitive <98>) <98>
IN	#40# Cyclohexanol (#40# competitive <275>) <275>
IN	#40# Disulfiram (#40# competitive <98>) <98>
IN	#40# 6-Thioguanine (#40# competitive <98>) <98>
IN	#40# propan-2-ol (#40# competitive <275>) <275>
IN	#40# Penicillamine (#40# competitive <98>) <98>
IN	#40# 1,4-dithiothreitol (#40# competitive <98>) <98>
IN	#40# Thiophenol (#40# competitive <98>) <98>
IN	#40# 2-mercaptobenzothiazole (#40# competitive <98>) <98>
IN	#40# 6-thioguanosine (#40# competitive <98>) <98>
IN	#40# 1,2-Ethanedithiol (#40# competitive <98>) <98>
IN	#40# 1-thiosorbitol (#40# competitive <98>) <98>
IN	#40# 1,3-propanedithiol (#40# competitive <98>) <98>
IN	#40# 1,4-dithioerythritol (#40# competitive <98>) <98>
IN	#40# 1,4-Butanedithiol (#40# competitive <98>) <98>
IN	#40# 1-thioglycerol (#40# competitive <98>) <98>
IN	#40# 1-thiobutane (#40# competitive <98>) <98>
IN	#40# 2-mercaptobenzimidazole (#40# competitive <98>) <98>
IN	#40# 2-thiobutane (#40# competitive <98>) <98>
IN	#40# 3-mercapto-1,2,4-triazole (#40# competitive <98>) <98>
IN	#40# 1,2-dithioglycerol (#40# competitive <98>) <98>
IN	#40# 1-hydroxypyridine-2-thione (#40# competitive <98>) <98>
IN	#40# 1-thio-1-phenylmethane (#40# competitive <98>) <98>
IN	#40# 1-thioacetamide (#40# competitive <98>) <98>
IN	#40# 1-thioacetate (#40# competitive <98>) <98>
IN	#40# 1-thioethane (#40# competitive <98>) <98>
IN	#40# 1-thiopropane (#40# competitive <98>) <98>
IN	#40# 2-mercapto-1-methylimidazole (#40# competitive <98>) <98>
IN	#40# 2-mercaptoimidazole (#40# competitive <98>) <98>
IN	#40# 2-phenylethanethiol (#40# competitive <98>) <98>
IN	#40# 2-pyridylethanethiol (#40# competitive <98>) <98>
IN	#40# 2-thioacetate (#40# competitive <98>) <98>
IN	#40# 2-thiopropane (#40# competitive <98>) <98>
IN	#40# 2-thiopyridine (#40# competitive <98>) <98>
IN	#40# 2-thiopyrimidine (#40# competitive <98>) <98>
IN	#40# 3-thiopropionate (#40# competitive <98>) <98>
IN	#40# 5-beta-D-ribofuranosylnicotinamide adenine dinucleotide (#40#
	potent and specific inhibitor <55>) <55>
IN	#40# NO (#40# Cys residues contained within the zinc/thiolate active
	center may be primary sites of NO interaction <102>) <102>
IN	#40# p-nitrophenol (#40# noncompetitive inhibition of the hydrolysis of
	p-nitrophenyl octanoate <39>) <39>
IN	#40# S-2-Chloro-3-(imidazol-5-yl)propionate (#40# inactivation at pH
	8.2, R-2-chloro-3-(imidazol-5-yl)propionate has no effect <29>) <29>
IN	#41# cyanide (#41# competitive with nicotinamide nucleotides. NADH
	increases cyanide-resistance of ADH II <140>) <140>
IN	#45# guanidine hydrochloride <154>
IN	#45# Iodine <163>
IN	#45# sodium iodoacetate (#45# increasing concentrations od sodium
	iodoacetate produce a slight decrease in activity <153>) <153>
IN	#45# o-phenanthroline (#45# loses 30% of its activity immediately on
	addition of o-phenanthroline <163>) <163>
IN	#46,91,100# NiCl2 (#100# 1 mM, complete inhibition <185>; #46# 1 mM,
	93% inhibition <149>; #91# 1 mM, 79% inhibition <144>) <144,149,185>
IN	#5# cyclohexylformamide (#5# dead-end inhibition pattern <110>) <110>
IN	#5# dodecanoic acid (#5# inhibits ADH3 irrespective of substrate <200>)
	<200>
IN	#5# caffeic acid (#5# mixed type of inhibition <212>) <212>
IN	#5# Vanillin (#5# mixed type of inhibition <212>) <212>
IN	#5# ellagic acid (#5# mixed type of inhibition <212>) <212>
IN	#5# syringaldehyde (#5# mixed type of inhibition <212>) <212>
IN	#5,40,86# Octanoic acid (#40# competitive inhibition of the hydrolysis
	of p-nitrophenyl octanoate <39>; #5# dead-end inhibition pattern <110>;
	#86# interacts with the catalytic zinc ion, binding structure <127>)
	<39,110,127>
IN	#5,7,8,26,33,35,40,42,45,65,72,78,105,108# 4-Methylpyrazole (#45#
	competitive inhibitor <163>; #8# 1 mM, 31% inhibition <23>; #8# class
	III enzyme is completely insensitive to inhibition <11,16>; #8# poor
	inhibitor, class II isoenzyme <14>; #8# no inhibition by 12 mM <21>;
	#8# competitive against ethanol <96>; #35# isoenzyme AA-ADH, BB-ADH and
	TT-ADH <95>; #5# inhibits cell protein carbonylation following exposure
	to crotyl alcohol <117>) <2,11,14,16,21,23,24,25,95,96,117,135,163,214>
IN	#5,8,12,18,25,35,41,42,67,72,78,91,100# 1,10-phenanthroline (#100# 1
	mM, complete inhibition <185>; #35# mixed type inhibition <47>; #91# 1
	mM, 38% inhibition <144>; #5# inhibition of isoenzyme A2 and C2, no
	inhibition of isoenzyme B2 <48>; #41# 0.2 mM, strong inhibition <68>;
	#25# 1 mM, 6% inhibition <188>)
	<2,14,21,24,25,45,47,48,68,69,75,95,144,185,188>
IN	#5,8,9,10,12,19,42,45,68,77,78,87# pyrazole (#77# competitive <38>;
	#87# strong inhibition <118>; #8# 0.05 mM, 50% inhibition <10>; #45#
	competitive inhibitor <163>; #77# competitive towards ethanol <61>; #9#
	0.1-10 mM, ADH-2 is practically insensitive, ADH-3 is very sensitive
	<49>; #9# 0.05 mM, complete inhibition <10>; #8# no inhibition at 1.0
	mM <23>; #42,78# organism has a pyrazole-sensitive isoenzyme and a
	pyrazole-insensitive enzyme <24,25>; #68# pyrazole-sensitive enzyme
	forms ADH-1, ADH-2, ADH-3 and the pyrazole-insensitive form ADH-An
	<60>; #5# inhibition of isoenzyme A2 and C2. Isoenzyme B2 is
	insensitive to pyrazole inhibition with trans-2-hexen-1-ol as substrate
	<48>) <10,12,23,24,25,38,45,48,49,60,61,71,94,118,163,212>
IN	#54# p-chloromercuribenzene sulfonate <99>
IN	#54,113,114# Mn2+ (#113# 1 mM, 14.3% residual activity <215>; #114# 1
	mM, 23.4% residual activity <215>) <99,215>
IN	#54,113,114,150# Co2+ (#150# 1 mM, 19% residual activity <244>; #113# 1
	mM, 51.9% residual activity <215>; #114# 1 mM, 68.7% residual activity
	<215>) <99,215,244>
IN	#54,98,113,114# Ni2+ (#98# 10 mM, 46% loss of activity <173>; #114# 1
	mM, 18.2% residual activity <215>; #113# 1 mM, 72.7% residual activity
	<215>) <99,173,215>
IN	#56,57# Ba2+ (#57# 5 mM, 95% inhibition <147>; #56# 5 mM, 94%
	inhibition <147>) <147>
IN	#56,57# Cr3+ (#57# 5 mM, 88% loss of activity <147>; #56# 5 mM, 84%
	loss of activity <147>) <147>
IN	#56,57# Zr2+ (#56# 5 mM, 78% inhibition <147>; #57# 5 mM, 72%
	inhibition <147>) <147>
IN	#56,57# Pb2+ (#57# 5 mM, 96% inhibition <147>; #56# 5 mM, 98%
	inhibition <147>) <147>
IN	#56,57# Li+ (#56# 5 mM, 28% inhibition <147>; #57# 5 mM, 32% inhibition
	<147>) <147>
IN	#56,57,123,150# Fe2+ (#123# 1 mM, 7% inhibition <218>; #56# 5 mM, 48%
	inhibition <147>; #57# 5 mM, 61% inhibition <147>; #150# 1 mM, 60%
	residual activity <244>) <147,218,244>
IN	#6# CaCl2 (#6# 100 mM, 30% inhibition <169>) <169>
IN	#6,100# MgCl2 (#100# 1 mM, 10% inhibition <185>; #6# 100 mM, 33%
	inhibition <169>) <169,185>
IN	#6,114# Ca2+ (#114# 1 mM, no residual activity <215>; #6# 100 mM, 70%
	of initial activity <169>) <169,215>
IN	#6,12,18,45,123# Hg2+ (#18# no effect <75>; #123# 1 mM, 63% of initial
	activity <219>; #6# 100 mM, 33% of initial activity <169>)
	<45,75,163,169,219>
IN	#6,12,18,96,113,114,123,150# Cu2+ (#18# no effect <75>; #96# 1 mM, 99%
	loss of activity <168>; #114# 1 mM, 14.0% residual activity <215>;
	#113# 1 mM, 44.2% residual activity <215>; #123# 1 mM, 89% of initial
	activity <219>; #150# 1 mM, no% residual activity <244>; #6# 100 mM,
	76% of initial activity <169>) <45,75,168,169,215,219,244>
IN	#6,123# 1-butyl-3-methylimidazolium tetrafluoroborate (#6# 2 mM, 65%
	inhibition <169>; #123# 5%, 50% inhibition, presumably due to a
	competition of the BF4- ion with the coenzyme phosphate moiety for the
	anion-binding site of the enzyme <218>; #6# 2 mM, 35% of initial
	activity <169>) <169,218>
IN	#6,18,113,114# Mg2+ (#114# 1 mM, 0.3% residual activity <215>; #113# 1
	mM, 74.3% residual activity <215>; #6# 100 mM, 67% of initial activity
	<169>) <76,169,215>
IN	#6,25,46,91,92,100,127# HgCl2 (#25,46,91,100# 1 mM, complete inhibition
	<144,149,185,188>; #127# complete inhibition at 1 mM <225>; #92# 0.1
	mM, 85% inhibition <137>; #6# 1 mM, 67% inhibition <169>)
	<137,144,149,169,185,188,225>
IN	#6,46,91,100# CuCl2 (#46,100# 1 mM, complete inhibition <149,185>; #6#
	1 mM, 24% inhibition <169>; #91# 1 mM, 68% inhibition <144>)
	<144,149,169,185>
IN	#67# NaN3 <69>
IN	#77# 2-Chloroethanol (#77# competitive towards ethanol <61>) <61>
IN	#77# Cibacron blue (#77# competitive towards NAD+ <61>) <61>
IN	#77# isoburyramide (#77# competitive towards ethanol and butan-2-ol
	<61>) <61>
IN	#8# NADP+ <21>
IN	#8# 4-bromopyrazole <23>
IN	#8# 4-pentylpyrazole <12,23>
IN	#8# sulfonic acid <21>
IN	#8# 8-Amino-6-methoxyquinoline <12>
IN	#8# 4-cyanopyrazole <23>
IN	#8# 4-nitropyrazole <23>
IN	#8# 4-octylpyrazole <12>
IN	#8# 4-propylpyrazole <23>
IN	#8# all-trans-retinal (#8# product inhibition <124>) <124>
IN	#8# 4-androsten-3,17-dione (#8# competitive against substrate
	cyclohexanone <116>) <116>
IN	#8# 3-butylthiolan 1-oxide (#8# dead-end inhibitor to the
	enzyme-cofactor complex, inhibition of oxidation reaction <116>) <116>
IN	#8# 5alpha-androstan-17beta-ol-3-one (#8# i.e.
	5alpha-dihydrotestosterone, allosteric, competitive against substrate
	cyclohexanone, noncompetitive against NAD+ nd ethanol <116>) <116>
IN	#8# N-cyclopentyl-N-cyclobutylformamide (#8# inhibits isozyme
	alphaalpha, complex structure <109>) <109>
IN	#8# N-benzylformamide (#8# inhibits isozyme beta(1)beta(1) <109>) <109>
IN	#8# N-heptylformamide (#8# inhibits isozyme beta(1)beta(1) <109>) <109>
IN	#8# N-1-methylheptylformamide (#8# inhibits isozyme gamma(2)gamma(2)
	<109>) <109>
IN	#8# all-trans-retinoic acid (#8# weak feedback inhibition <124>) <124>
IN	#8# cimetidine (#8# 0.2 mM, 2.5% inhibition of hepatic allotype
	ADH1B*1/*1 activity, 12% inhibition of hepatic allotype ADH1B*2/*2
	activity <273>) <273>
IN	#8# acetaminophen (#8# 0.5 mM, 16% inhibition of hepatic allotype
	ADH1B*1/*1 activity, 6.1% inhibition of hepatic allotype ADH1B*2/*2
	activity <273>) <273>
IN	#8# Acetylsalicylate (#8# 1 mM, 4.4% inhibition of hepatic allotype
	ADH1B*1/*1 activity, 2.8% inhibition of hepatic allotype ADH1B*2/*2
	activity <273>) <273>
IN	#8# salicylate (#8# 1.5 mM, 12% inhibition of hepatic allotype
	ADH1B*1/*1 activity, 31% inhibition of hepatic allotype ADH1B*2/*2
	activity <273>) <273>
IN	#8,10# trifluoroethanol (#8# competitive against retinol,
	noncompetitive against NAD+ <124>) <91,124>
IN	#8,10,78# dipicolinic acid (#10# Zn2+ chelator and inhibitor of ADH
	<209>) <21,24,209>
IN	#8,18,25,42,45,47,54,56,57,60,78,111,123# EDTA (#25# 1 mM, 31%
	inhibition <188>; #45# 15 mM, 85% inhibition <66>; #60# 67% inhibition
	of ADH II at 5 mM, 45% inhibition of ADH I at 1 mM, irreversible
	inhibition, addition of Mg2+ and Zn2+ increase the inhibitory effect
	<113>; #57# 25% inhibition at 10.5 mM, 44% inhibition at 21 mM <147>;
	#56# 31% inhibition at 10.5 mM, 92% inhibition at 21 mM <147>; #45#
	loses 30% of its activity immediately on addition of EDTA <163>; #111#
	2.3% relative activity at 10 mM <197>; #123# 1 mM, 93% of initial
	activity <219>) <14,24,25,66,76,99,113,147,163,188,197,219,223>
IN	#8,40# Isobutyramide (#8# substrate inhibition, competitive against
	retinol, noncompetitive against NADH <124>) <124,175>
IN	#8,42# 2,2'-bipyridine <14,25>
IN	#8,45# 4-iodopyrazole (#45# competitive inhibitor <163>) <23,163>
IN	#8,78# 8-hydroxyquinoline 5-sulfonic acid <21,24>
IN	#8,9,10,12,35# 4-methoxypyrazole (#35# competitive <47>; #8# 1 mM, 28%
	inhibition <23>; #12# class I ADHs migrate towards cathode on starch
	gel and are very sensitive to 4-methylpyrazole inhibition, class II ADH
	migrates slowly towards anode and is less sensitive to
	4-methylpyrazole, class II ADH migrates rapidly towards anode and is
	insensitive to 4-methylpyrazole <46>; #9# 0.1-10 mM, ADH-2 is
	practically insensitive, ADH-3 is very sensitive <49>; #9# competitive
	inhibitor of all four isoenzymes <51>) <23,45,46,47,49,51,53,91>
IN	#8,98,111# Tween 80 (#8# competitive, stabilizes the retinoid
	compounds, elevates the Km values of the substrates, most effective at
	0.1% w/v <107>; #98# 10% (w/v), 89% inhibition <173>; #111# 13%
	relative activity at 10% (v/v) <197>) <107,173,197>
IN	#87# trichloroethanol (#87# weak inhibition <118>) <118>
IN	#89# NAD+ (#89# substrate inhibition above 5 mM <105>) <105>
IN	#89,98,105,108# ethanol (#89# substrate inhibition above 0.5 M <105>;
	#98# 50% (v/v), 59% loss of activity <173>; #105# ethanol competitively
	inhibits the oxidation of 1-hydroxymethylpyrene by ADH1C and ADH3
	<214>; #108# ethanol competitively inhibits the oxidation of
	1-hydroxymethylpyrene by ADH4 <214>) <105,173,214>
IN	#91# polyoxyethylene octylphenyl ether (#91# 1 mM, 43% inhibition
	<144>) <144>
IN	#91# FeCl2 (#91# 1 mM, 57% inhibition <144>) <144>
IN	#91# Hydroxylamine hydrochloride (#91# 1 mM, 34% inhibition <144>) <144>
IN	#91# hexadecyltrimethyl-ammonium bromide (#91# 1 mM, 79% inhibition
	<144>) <144>
IN	#92# KCN (#92# 1 mM, 41% inhibition <137>) <137>
IN	#92,100# FeCl3 (#92# 1 mM, 34% inhibition <137>; #100# 0.1 mM, 13%
	inhibition <185>) <137,185>
IN	#98# pefabloc (#98# 10 mM, 32% inhibition <173>) <173>
IN	#98# Na+ (#98# 10 mM, 13% loss of activity <173>) <173>
IN	#98# CHAPS (#98# 10% (w/v), 59% inhibition <173>) <173>
IN	#98# Triton X-100 (#98# 10% (w/v), 78% inhibition <173>) <173>
IN	#98# Tween 20 (#98# 10% (w/v), 82% inhibition <173>) <173>
IN	#98# methanol (#98# 50% (v/v), 30% loss of activity <173>) <173>
IN	#98# hexadecane (#98# 50% (v/v), 71% loss of activity <173>) <173>
IN	#98# Isopropanol (#98# 50% (v/v), 88% loss of activity <173>) <173>
IN	#98# tert-butanol (#98# 50% (v/v), 92% loss of activity <173>) <173>
IN	#98# Toluene (#98# 50% (v/v), 97% loss of activity <173>) <173>
IN	#98# isooctane (#98# 50% (v/v), 98% loss of activity <173>) <173>
IN	#98# heptane (#98# 50% (v/v), 99% loss of activity <173>) <173>
IN	#98,105,108# DMSO (#98# 50% (v/v), 29% loss of activity <173>; #105#
	DMSO inhibits isozyme ADH2-catalysed oxidation in an uncompetitive mode
	and reduction in a mixed mode <214>; #105# DMSO inhibits isozymes
	ADH1C-catalysed oxidation in an uncompetitive mode and reduction in a
	mixed mode, no inhibition is detected with isozyme ADH3 <214>; #108#
	DMSO inhibits isozymes ADH4-catalysed oxidation in an uncompetitive
	mode and reduction in a mixed mode <214>) <173,214>
IN	#98,111# Urea (#98# 5 M, 41% inhibition <173>; #111# 1% relative
	activity at 5 M <197>) <173,197>
IN	#98,113,114# Al3+ (#98# 10 mM, 30% loss of activity <173>; #114# 1 mM,
	14.7% residual activity <215>; #113# 1 mM, 18.9% residual activity
	<215>) <173,215>
IN	#98,113,114# K+ (#98# 10 mM, 29% loss of activity <173>; #113# 1 mM,
	70.3% residual activity <215>; #114# 1 mM, 82.3% residual activity
	<215>) <173,215>

KI_VALUE
KI	#10# 20.8 {5-hydroxymethylfurfural}  (#10# mutant S110P/Y295C, pH 6.7,
	30°C <282>) <282>
KI	#10# 0.025 {mithramycin}  (#10# in 50 mM Tris-HCl, pH 8.0 at 25°C
	<209>) <209>
KI	#10# 0.038 {mithramycin}  (#10# in 50 mM Tris-HCl, pH 8.0 at 25°C
	<209>) <209>
KI	#10# 46 {acetaldehyde}  (#10# mutant S110P/Y295C, pH 6.7, 30°C <282>)
	<282>
KI	#10# 1.32 {furfural}  (#10# mutant S110P/Y295C, pH 6.7, 30°C <282>)
	<282>
KI	#10# 12.53 {acetaldehyde}  (#10# wild-type, pH 6.7, 30°C <282>) <282>
KI	#10# 1363 {furfural}  (#10# wild-type, pH 6.7, 30°C <282>) <282>
KI	#105# 1.7 {ethanol}  (#105# isozyme ADH1C, using 1-hydroxymethylpyrene
	as substrate <214>) <214>
KI	#105# 1470 {ethanol}  (#105# isozyme ADH3, using 1-hydroxymethylpyrene
	as substrate <214>) <214>
KI	#108# 3.3 {ethanol}  (#108# isozyme ADH4, using 1-hydroxymethylpyrene
	as substrate <214>) <214>
KI	#118# 2.1 {Butyraldehyde}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KI	#26# 6.64 {4-Methylpyrazole}  <135>
KI	#33# 0.47 {4-Methylpyrazole}  <135>
KI	#40# 9.7 {Cyclohexanol}  (#40# pH 8.0, 25°C <275>) <275>
KI	#40# 96 {propan-2-ol}  (#40# pH 8.0, 25°C <275>) <275>
KI	#45# 0.13 {pyrazole}  (#45# apparent value <163>) <163>
KI	#45# 0.009 {4-Methylpyrazole}  (#45# apparent value <163>) <163>
KI	#45# 0.0032 {4-iodopyrazole}  (#45# apparent value <163>) <163>
KI	#5# 0.026 {Octanoic acid}  (#5# pH 7.5, 25°C, wild-type enzyme, versus
	NAD+ <110>) <110>
KI	#5# 0.072 {cyclohexylformamide}  (#5# pH 7.5, 25°C, wild-type enzyme,
	versus NADH <110>) <110>
KI	#5# 0.00008 {caffeic acid}  (#5# at 37°C in 0.1 M Na-K phosphate
	buffer (pH 7.4) <212>) <212>
KI	#5# 0.0051 {pyrazole}  (#5# at 37°C in 0.1 M Na-K phosphate buffer (pH
	7.4) <212>) <212>
KI	#5# 0.022 {ellagic acid}  (#5# at 37°C in 0.1 M Na-K phosphate buffer
	(pH 7.4) <212>) <212>
KI	#5# 0.035 {cyclohexylformamide}  (#5# pH 7.5, 25°C, wild-type enzyme,
	versus benzaldehyde <110>) <110>
KI	#5# 0.037 {Octanoic acid}  (#5# pH 7.5, 25°C, wild-type enzyme, versus
	octanol <110>) <110>
KI	#5# 0.0079 {Vanillin}  (#5# at 37°C in 0.1 M Na-K phosphate buffer (pH
	7.4) <212>) <212>
KI	#5# 0.0156 {syringaldehyde}  (#5# at 37°C in 0.1 M Na-K phosphate
	buffer (pH 7.4) <212>) <212>
KI	#65# 6.4 {4-Methylpyrazole}  <135>
KI	#7# 18.26 {4-Methylpyrazole}  <135>
KI	#8# 0.014 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	versus ethanol <116>) <116>
KI	#8# 0.028 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	versus NAD+ <116>) <116>
KI	#8# 0.0047 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	versus cyclohexanone <116>) <116>
KI	#8# 0.0047 {4-androsten-3,17-dione}  (#8# pH 7.3, 37°C, versus
	cyclohexanone <116>) <116>
KI	#8,23# -999 {more}  (#8# inhibition kinetics <116>) <116,123,124>

METALS_IONS
ME	#10# Ca2+ (#10# CaCl2 and MgCl2 are able to stabilize the enzyme at
	millimolar concentrations. Ca2+ stabilizes yeast ADH I by preventing
	the dissociation of the reduced form of the enzyme and by preventing
	the unfolding of the oxidized form of the enzyme. Ca2+ is fixed by the
	Asp236 and Glu101 side chains in yeast ADH I <247>; #10# 0.5 mM,
	substrate glycolaldehyde, 86.2% residual activity <285>) <247,285>
ME	#10# Fe3+ (#10# 0.5 mM, substrate glycolaldehyde, 92.2% residual
	activity <285>) <285>
ME	#10,123,148# Mn2+ (#148# stimulation <241>; #123# 1 mM, 1.1 fold
	activation <218>; #10# 0.5 mM, substrate glycolaldehyde, 89% residual
	activity <285>) <218,241,285>
ME	#10,148# Co2+ (#148# stimulation <241>; #10# construction of an active
	metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which
	maintain the same configuration as the native zinc ion, but possessing
	a wider pH range and a lower activity and substrate affinity than the
	wild-type enzyme, overview <122>) <122,241>
ME	#10,25,148# Cu2+ (#148# stimulation <241>; #10# construction of an
	active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+,
	which maintain the same configuration as the native zinc ion, but
	possessing a wider pH range and a lower activity and substrate affinity
	than the wild-type enzyme, overview <122>; #25# 1 mM CuSO4, 1.7fold
	activation <188>; #10# 0.25 mM, substrate glycolaldehyde, no residual
	activity <285>) <122,188,241,285>
ME	#10,25,47,123# Ni2+ (#25# 1 mM NiSO4, 1.2fold activation <188>; #47#
	activates, the activity using 1,3-propanediol as substrate is highly
	dependent on the addition of NiCl2, while no change in activity is
	observed using ethanol in a sample with NiCl2 <223>; #123# 1 mM, 106%
	of initial activity <219>; #10# 0.5 mM, substrate glycolaldehyde, 54.9%
	residual activity <285>) <188,219,223,285>
ME	#10,47,51,148# Mg2+ (#51# enhances activity <82>; #148# stimulation
	<241>; #47# 40% activation at 10 mM <223>; #10# 0.5 mM, substrate
	glycolaldehyde, 93.5% residual activity <285>) <82,211,223,241,285>
ME	#104# selenium (#104# steady-state fluorescence properties of alcohol
	dehydrogenase and its selenomethionyl derivative <220>; #104# the
	effect of significant decrease in intrinsic fluorescence intensity of
	the enzyme caused by replacement of S atoms of methionine residues to
	Se is explained on the basis of the analysis of its 3D structure. All
	selenium atoms are located far from both Trp95 and Trp117 and can not
	cause their fluorescence quenching. Substitution of S by Se causes
	enhanced protein absorption in the UV-region. This effect is explained
	by the formation of Se complex with some groups of protein <221>)
	<220,221>
ME	#150# Ba2+ (#150# 1 mM, 113% of initial activity <244>) <244>
ME	#30# NaCl (#30# most active at 5 M NaCl or 4 M KCl <181>) <181>
ME	#30,132# KCl (#30# most active at 5 M NaCl or 4 M KCl <181>; #132#
	optimally active with ethanol and 1-propanol at pH 11.0 with 3 M KCl
	and with 1-butanol at pH 10.0 with 4 M KCl. Catalyzes the reductive
	reaction optimally at pH 6.0 with 4 M KCl <237>) <181,237>
ME	#42# copper (#42# contains 0.5 mol of copper per mol of enzyme <25>)
	<25>
ME	#47,110,111,113,114,148# more (#110# Mg2+ does not have any effect on
	activity <213>; #111# not stimulated by 10 mM Li+, Mg2+, Co2+, and Ca2+
	<197>; #113,114# enzyme contains neither Fe nor other metals, and Fe is
	not required for the activity, although sequence analysis reveals that
	ADH1 belongs to the Fe-containing/activated long-chain alcohol
	dehydrogenases <215>; #47# Adh3 exhibits tolerance to several metal
	ions <223>; #148# alcohol dehydrogenase activity is stimulated by a
	range of divalent metal ions, while aldehyde dehydrogenase activity is
	not <241>) <197,213,215,223,241>
ME	#5,6,8,10,13,25,26,40,43,45,60,86,93,109,110,121,148# Zn2+ (#10#
	activates <87>; #109# dependent on <210>; #45# zinc-containing
	metalloenzyme <164>; #5,40,86# catalytic zinc ion <110,111,127>; #45#
	zinc-containing enzyme <161>; #5# 1 catalytic and 1 structural zinc ion
	per subunit <119>; #26# 1 catalytic and 1 structural zinc ion per
	subunit, coordination complex geometry <129>; #13# 1 catalytic zinc ion
	and 1 structural zinc ion per enzyme subunit <112>; #43# 1 tightly
	bound ion per subunit <114>; #60# ADH I contains 1 Zn2+ per subunit,
	while ADH II does not contains any metal ions <113>; #10# all isozymes,
	amino acid residues involved in zinc in binding are Cys46, Cys174,
	His67, Glu68, Asp49, and Thr48, binding mode <120>; #8# catalytic zinc
	<109>; #10# included into the crystal strcuture <104>; #10# native
	enzyme contains catalytic zinc ions <122>; #45# the catalytic active
	site zinc ion is bound to Glu69 in the apoenzyme state, but not in the
	ternary complex state <108>; #93# ADH is a putative zinc-dependent
	alcohol dehydrogenase <162>; #45# contains a zinc ion which is directly
	involved in the structural stabilization of enzyme molecule <155>; #45#
	contains eight zinc atoms per tetramer <163>; #6# 1 mM ZnSO4, 1.14fold
	activation <169>; #25# 1 mM ZnSO4, 1.3fold activation <188>; #5# 2
	atoms are included in each 40 kDa subunit, while one of the zinc ions
	is considered to serve a structural function only, the other zinc ion
	functions as a Lewis acid and activates the substrate in the active
	site, which is located in a cleft between the catalytic and the
	coenzyme binding domain <200>; #10# contains Zn2+ <209>; #110# maximum
	activity is reached at 0.5 mM Zn2+,Ta1316 ADH is able to tolerate high
	concentrations of Zn2+ <213>; #40# zinc metalloenzyme with two zinc
	atoms per subunit <201>; #121# the enzyme likely contains 2 Zn2+ <217>;
	#6# 1 mM, 114% of initial activity <169>; #148# stimulation. Crystal
	structure of alcohol dehydrogenase domain contains 0.43 Zn atoms per
	protein monomer <241>; #10# 0.5 mM, substrate glycolaldehyde, 32.9%
	residual activity <285>)
	<87,104,108,109,110,111,112,113,114,119,120,122,127,129,155,161,162,163
	164,169,188,200,201,209,210,211,213,217,241,285>
ME	#5,8,9,12,14,18,35,40,41,42,45,54,67,78,102,103,104# Zinc (#104# zinc
	enzyme <220>; #18# required for activity, tightly bound within the
	enzyme <75>; #5# isoenzyme A2 contains 2.7 mol of zinc per mol of
	enzyme, isoenzyme b2 contains 1.9 mol of zinc per mol of enzyme,
	isoenzyme C2 contains 3.2 mol of zinc per mol of enzyme. A and C
	subunits each contain two atoms of zinc, with at least one being
	involved catalytically, the b subunit probably contains a single
	non-catalytic zinc atom <48>; #9# ADH-1 contains 3.9 mol of zinc per
	mol of subunit, ADH-2 contains 4.2 mol of zinc per mol of subunit <49>;
	#8# enzyme contains 7.59 zinc atoms per molecule <96>; #78# contains
	3.9 gatom of zinc per mol of enzyme <24>; #45# 2 mM required for
	optimal activity <66>; #40# substitution of catalytic and /or
	noncatalytic zinc ions by cobaltous ions <36>; #40# contains 4 zinc
	atoms per molecule <42>; #8,12# contains 3.8 mol of Zn per mol of
	protein <16,45>; #41# enzyme form ADH I and ADH II contain one zinc
	atom per subunit <67>; #14# contains 1 zinc atom per subunit <81>; #35#
	isoenzyme AA-ADH contains 4.3 zinc atoms per dimeric molecule,
	isoenzyme BB-ADH contains 3.7 zinc atoms per dimeric molecule,
	isoenzyme AA-ADH contains 4.1 zinc atoms per dimeric molecule <95>;
	#54# contains 1.2 Zn atom per subunit <99>; #67# contains 4 zinc atoms
	per dimer <69>; #8# zinc containing enzyme <12>; #8# from beta1gamma1
	and gamma1gamma1 isoenzyme the active-site zinc is extracted much more
	slowly than from beta1beta1 isoenzyme. Characterization of
	active-site-specific zinc-depleted and reconstituted cobalt(II) alcohol
	dehydrogenase <19>; #8# contains 3.7 gatom of zinc per mol of enzyme
	<23>; #8# 3.6-4.2 gatom of zinc per mol <21>; #42# contains 3.7-4.2 mol
	of zinc per mol of enzyme <25>; #102# KmADH3 appears to belong to the
	zinc-containing Adh family <177>; #103# KmADH4 appears to belong to the
	zinc-containing Adh family <177>)
	<12,16,19,21,23,24,25,36,42,45,48,49,66,67,69,70,75,81,95,96,99,177,220>
ME	#51,113,114,148# Fe2+ (#51# enhances activity <82>; #148# stimulation
	<241>; #113# 1 mM, 136% of initial activity <215>; #114# 1 mM, 168% of
	initial activity <215>) <82,215,241>
ME	#6# K+ (#6# 100 mM KCl, 1.9fold activation <169>; #6# 100 mM, 193% of
	initial activity <169>) <169>
ME	#6,25,123# Li+ (#25# 1 mM LiCl, 1.1fold activation <188>; #6# 100 mM
	LiCl, 1.8fold activation <169>; #123# 1 mM, 1.15fold activation <218>;
	#6# 100 mM, 178% of initial activity <169>) <169,188,218>
ME	#6,47,113,123# Na+ (#47# 40% activation at 1 mM <223>; #6# 100 mM NaCl,
	1.8fold activation <169>; #113# 1 mM, 110% of initial activity <215>;
	#123# 1 mM, 1.13fold activation <218>; #6# 100 mM, 179% of initial
	activity <169>) <169,215,218,223>
ME	#91# Zn (#91# the enzyme contains 2 gram-atoms Zn per subunit <144>)
	<144>

MOLECULAR_WEIGHT
MW	#1,8,9,10,35,41,52,78,79,91,105,108,111,130,131# 40000 (#111# SDS-PAGE
	<197>; #105# isozyme ADH2, apparent molecular weight deduced from
	electrophoretic mobility <214>; #108# isozyme ADH4, calculated from
	amino acid sequence <214>; #91,131# 4 * 40000, SDS-PAGE <144,239>;
	#8,10,35,52,78# 2 * 40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,79,130# x
	* 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, ADH-3, SDS-PAGE <49>;
	#41# 2 * 40000, enzyme form ADHI <68>)
	<11,16,23,24,44,49,52,59,68,87,95,144,197,214,227,239>
MW	#10# 60000-80000 (#10# gel filtration <87>) <87>
MW	#102# 37066 (#102# x * 37066, calculated <177>) <177>
MW	#103# 37311 (#103# x * 37311, calculated <177>) <177>
MW	#105# 39500 (#105# isozyme ADH3, apparent molecular weight deduced from
	electrophoretic mobility <214>) <214>
MW	#105# 39870 (#105# isozyme ADH1C, calculated from amino acid sequence
	<214>) <214>
MW	#105# 39720 (#105# isozyme ADH3, calculated from amino acid sequence
	<214>) <214>
MW	#105# 40220 (#105# isozyme ADH2, calculated from amino acid sequence
	<214>) <214>
MW	#105,108# 40500 (#105# isozyme ADH1C, apparent molecular weight deduced
	from electrophoretic mobility <214>; #108# isozyme ADH4, apparent
	molecular weight deduced from electrophoretic mobility <214>) <214>
MW	#106# 100000 (#106# SDS-PAGE <195>) <195>
MW	#110# 36010 (#110# 4 * 36010, Ta1316 ADH, calculated from amino acid
	sequence <213>) <213>
MW	#111# 37200 (#111# calculated molecular weight <197>) <197>
MW	#113# 380000 (#113# PAGE <215>) <215>
MW	#113# 41664 (#113# 8 * 45000, SDS-PAGE, 8 * 41664, calculated <215>)
	<215>
MW	#114# 90000 (#114# PAGE <215>) <215>
MW	#118# 158000 (#118# gel filtration <256>) <256>
MW	#12# 74500 (#12# gel filtration <46>) <46>
MW	#12# 41700 (#12# 2 * 41700, enzyme form CM-I: a polypeptide chain + C
	polypeptide chain, enzyme form CM-II: B-chain + C-chain, enzyme form CM
	III, homodimer of C chains, SDS-PAGE <46>) <46>
MW	#12,43# 72000 (#12# gel filtration <45>; #43# recombinant enzyme
	expressed from Arxula adeninivorans and Saccharomyces cerevisiae, gel
	filtration <232>) <45,232>
MW	#12,93,110# 36000 (#93# deduced from amino acid sequence <162>; #12# 2
	* 36000, SDS-PAGE <45>; #110# 4 * 36000, Ta1316 ADH, SDS-PAGE <213>)
	<45,162,213>
MW	#121# 133000 (#121# gel filtration <217>) <217>
MW	#121# 37477 (#121# 4 * 37477, calculeted from sequence <217>) <217>
MW	#122,123# 28978 (#122# 4 * 28978, calculated from sequence <219>; #123#
	4 * 28978, calculated, 4 * 30000, SDS-PAGE <219>) <219>
MW	#123# 65000 (#123# gel filtration <219>) <219>
MW	#123# 109000 (#123# sucrose density gradient centrifugation <218>) <218>
MW	#123# 27024 (#123# 4 * 27024, ESI-MS analysis <218>) <218>
MW	#127# 28900 (#127# 2 * 28900, SDS-PAGE <225>) <225>
MW	#127# 59900 (#127# gel filtration <225>) <225>
MW	#131# 39570 (#131# 4 * 39570, calculated from sequence <239>) <239>
MW	#132# 138000 (#132# gel filtration <237>) <237>
MW	#132# 37600 (#132# 4 * 37600, SDS-PAGE <237>) <237>
MW	#135,136,137# 190000 (#135,136,137# gel filtration <252>) <252>
MW	#135,136,137# 48000 (#135,136,137# 4 * 48000, SDS-PAGE <252>) <252>
MW	#138# 200000 (#138# gel filtration <252>) <252>
MW	#138# 49000 (#138# 4 * 49000, SDS-PAGE <252>) <252>
MW	#14# 290000 (#14# gel filtration <81>) <81>
MW	#14# 37500 (#14# x * 37500, SDS-PAGE <81>) <81>
MW	#142# 32000 (#142# 1 * 32000, SDS-PAGE <138>) <138>
MW	#148# 99000 (#148# alcohol dehydrogenase domain, dynamic
	light-scattering <241>) <241>
MW	#148# 48600 (#148# 2 * 48600, alcohol dehydrogenase domain, SDS-PAGE.
	Unlike the native ADHE, the alcohol dehydrogenase domain alone does not
	assemble into spirosome structures <241>) <241>
MW	#149# 27000 (#149# gel filtration <243>) <243>
MW	#149# 31464 (#149# 1 * 31000, SDS-PAGE, 1 * 31464, calculated <243>)
	<243>
MW	#15# 37983 (#15# x * 37983, ADH3, calculated from sequence <172>) <172>
MW	#150# 36411 (#150# x * 36411, calculated, x * 37000, SDS-PAGE <244>)
	<244>
MW	#157# 91480 (#157# calculated from sequence <283>) <283>
MW	#16# 89000-91000 (#16# gel filtration <79>) <79>
MW	#16,51,56,113# 45000 (#56# gel filtration <147>; #16# 2 * 45000,
	SDS-PAGE <79>; #51# 4 * 45000, SDS-PAGE <82>; #113# 8 * 45000,
	SDS-PAGE, 8 * 41664, calculated <215>) <79,82,147,215>
MW	#18,45,60# 70000 (#18# gel filtration <75>; #45# gel filtration,
	sucrose density gradient centrifugation <66>; #60# ADH II, grl
	filtration <113>) <66,75,113>
MW	#18,45,94,98# 35000 (#18# 2 * 35000, SDS-PAGE <75>; #45,94# 4 * 35000,
	gel filtration <159>; #98# 12 * 35000, SDS-PAGE <173>) <75,159,173>
MW	#19,45,47# 74000 (#45# gel filtration, sucrose density gradient
	centrifugation <70>; #19# gel filtration sedimentation equilibrium
	centrifugation <71>; #47# recombinant His-tagged enzyme, gel filtration
	<223>) <70,71,223>
MW	#20# 70000-80000 (#20# gel filtration <284>) <284>
MW	#21# 68000 (#21# gel filtration <72>) <72>
MW	#21,45,118,150# 37000 (#118# 4 * 37000, SDS-PAGE <256>; #21,45# 2 *
	37000, SDS-PAGE <66,70,72,165>; #150# x * 36411, calculated, x * 37000,
	SDS-PAGE <244>) <66,70,72,165,211,244,256>
MW	#23,148# 96000 (#23# x * 96000, SDS-PAGE <128>; #148# x * 96000,
	wild-type, SDS-PAGE <241>) <128,241>
MW	#24# 31997 (#24# x * 31997, amino acid sequence calculation <106>) <106>
MW	#25,66,80# 58000 (#25# gel filtration <188>; #66,80# 2 * 58000,
	SDS-PAGE <77,78>) <77,78,188>
MW	#25,72,77# 28000 (#25,77# 2 * 28000, SDS-PAGE <61,188>; #72# x * 28000,
	SDS-PAGE <2>) <2,61,188>
MW	#3,84,96,122,123,142# 30000 (#96,142# gel filtration <138,168>; #122# 4
	* 30000, SDS-PAGE <219>; #84# x * 30000, SDS-PAGE <226>; #3# 2 * 30000
	<4>; #123# 4 * 28978, calculated, 4 * 30000, SDS-PAGE <219>)
	<4,138,168,219,226>
MW	#30# 41300 (#30# x * 41300, SDS-PAGE <181>) <181>
MW	#31,128,154# 150000 (#31,128,154# gel filtration <73,230,271>)
	<73,230,271>
MW	#37# 152000 (#37# gel filtration <85>) <85>
MW	#37,41,43,121,128# 38000 (#43# 2 * 38000, SDS-PAGE <114>; #37,121# 4 *
	38000, SDS-PAGE <85,217>; #41# 2 * 38000, enzyme form ADHII, SDS-PAGE
	<68>; #43# 2 * 38000, recombinant enzyme, SDS-PAGE <232>; #128# 4 *
	38000, calculated from sequence <230>) <68,85,114,217,230,232>
MW	#4# 55600 (#4# gel filtration <64>) <64>
MW	#4,71,74# 27800 (#4,71,74# 2 * 27800, SDS-PAGE <64>) <64>
MW	#41# 95000 (#41# enzyme form ADHII, gel filtration <68>) <68>
MW	#41# 145000 (#41# enzyme form ADH-I, glycerol density gradient
	centrifugation <67>) <67>
MW	#41# 67000 (#41# enzyme form ADH-II, glycerol density gradient
	centrifugation <67>) <67>
MW	#41# 34700 (#41# 2 * 34700, enzyme form ADH-I, SDS-PAGE <67>) <67>
MW	#41# 31100 (#41# 2 * 31100, enzyme form ADH-II, SDS-PAGE <67>) <67>
MW	#42# 76000-77000 (#42# equilibrium sedimentation <25>) <25>
MW	#43# 66000 (#43# recombinant enzyme expressed from Hansenula
	polymorpha, gel filtration <232>) <232>
MW	#44# 46000 (#44# 2 * 46000, SDS-PAGE <6>) <6>
MW	#44,148# 86000 (#148# alcohol dehydrogenase domain, gel filtration
	<241>) <6,241>
MW	#45# 135000 (#45# SDS-PAGE <163>) <163>
MW	#45# 150300 (#45# electrospray mass spectrometry <154>) <154>
MW	#45# 37585 (#45# 4 * 37585, electrospray mass spectrometry <154>) <154>
MW	#45# 37588 (#45# 4 * 37588, calculated from amino acid sequence <163>)
	<163>
MW	#45# 37591 (#45# 4 * 37591, electrospray mass spectrometry <163>) <163>
MW	#45,94# 140000 (#45,94# gel filtration <159>) <159>
MW	#46,123# 29000 (#46# gel filtration <149>; #123# 4 * 29000, SDS-PAGE
	<218>) <149,218>
MW	#5# 85000 (#5# isoenzyme C2, gel filtration <48>) <48>
MW	#5# 47000 (#5# 2 * 47000, isoenzyme C2, SDS-PAGE <48>) <48>
MW	#5# 83000 (#5# isoenzyme A2, gel filtration <48>) <48>
MW	#5# 79000 (#5# isoenzyme B2, gel filtration <48>) <48>
MW	#5,9,46# 39000 (#46# 1 * 39000, SDS-PAGE <149>; #5# 2 * 39000,
	isoenzyme B2, SDS-PAGE <48>; #9# 2 * 39000, ADH-2, SDS-PAGE <49>)
	<48,49,149>
MW	#5,9,54,87# 43000 (#87# 2 * 43000, SDS-PAGE <118>; #9# 2 * 43000,
	ADH-1, SDS-PAGE <49>; #5# 2 * 43000, isoenzyme A2, SDS-PAGE <48>; #54#
	10 * 43000, SDS-PAGE <99>) <48,49,99,118>
MW	#50# 400000 (#50# gel filtration <279>) <279>
MW	#51# 180000 (#51# gel filtration <82>) <82>
MW	#54# 320000 (#54# gel filtration <99>) <99>
MW	#57# 25000 (#57# gel filtration <147>) <147>
MW	#57# 24600 (#57# 1 * 24600, SDS-PAGE <147>) <147>
MW	#6# 105000 (#6# buffer containing 25 mM NaCl, gel filtration <169>)
	<169>
MW	#6# 26961 (#6# 4 * 26961, calculated from sequence <169>) <169>
MW	#60# 130000 (#60# ADH I, gel filtration <113>) <113>
MW	#60,96,125,149# 31000 (#96# 1 * 31000, SDS-PAGE <168>; #60# 2 * 31000,
	ADH II, SDS-PAGE <113>; #125# x * 31000, recombinant His6-tagged
	enzyme, SDS-PAGE <231>; #149# 1 * 31000, SDS-PAGE, 1 * 31464,
	calculated <243>) <113,168,231,243>
MW	#66,80# 116000 (#66,80# gel filtration <77,78>) <77,78>
MW	#67# 94000 (#67# gel filtration <69>) <69>
MW	#68# 82750 (#68# enzyme form ADH-3, equilibrium sedimentation <60>) <60>
MW	#69# 176000 (#69# non-denaturing PAGE <84>) <84>
MW	#71# 54600 (#71# gel filtration <64>) <64>
MW	#74# 57600 (#74# gel filtration <64>) <64>
MW	#77# 56000 (#77# gel filtration <61>) <61>
MW	#78# 77330 (#78# equilibrium sedimentation <24>) <24>
MW	#8# 78000 (#8# ultracentrifugation under non-denaturing conditions
	<23>) <23>
MW	#8# 78000-85000 (#8# amino acid analysis, ultracentrifugation <18>) <18>
MW	#8# 79000-84000 (#8# ultracentrifugal analysis <21>) <21>
MW	#8# 82700 (#8# equilibrium sedimentation <16>) <16>
MW	#8,35# 41000 (#35# 2 * 41000, SDS-PAGE <47>; #8# 2 * 41000, class III
	isoenzyme chi ADH, SDS-PAGE <16>) <16,47>
MW	#8,60,67,68,69# 42000 (#69# 4 * 42000, SDS-PAGE <84>; #8# x * 42000,
	SDS-PAGE <14>; #67# 2 * 42000, SDS-PAGE <69>; #8# 2 * 42000, anodic
	enzyme form, SDS-PAGE <18>; #68# 2 * 42000, enzyme form ADH-2 and
	ADH-3, SDS-PAGE <60>; #60# 3 * 42000, ADH I, SDS-PAGE <113>)
	<14,18,60,69,84,113>
MW	#87# 88000 (#87# approximately, gel filtration <118>) <118>
MW	#9,35,41,52# 80000 (#9,35,52# gel filtration <47,49,59,95>; #41# enzyme
	form ADHI, gel filtration <68>) <47,49,59,68,95>
MW	#91,131# 160000 (#91,131# gel filtration <144,239>) <144,239>
MW	#92# 110000 (#92# gel filtration <137>) <137>
MW	#92# 26000 (#92# 4 * 26000, SDS-PAGE <137>) <137>
MW	#95# 57000 (#95# SDS-PAGE <156>) <156>
MW	#95# 56700 (#95# deduced from amino acid sequence <156>) <156>
MW	#97# 37443 (#97# x * 37443, ADH1, calculated from sequence <172>) <172>
MW	#99# 81500 (#99# gel filtration <171>) <171>
MW	#99# 36900 (#99# 2 * 36900, SDS-PAGE <171>) <171>

POSTTRANSLATIONAL_MODIFICATION
PM	#102,103# proteolytic modification (#102# sequence contains a
	N-terminal mitochondrial import sequence of 24 amino acids <177>; #103#
	sequence contains a N-terminal mitochondrial import sequence of 28
	amino acids <177>) <177>
PM	#45# more (#45# carboxymethylation with sodium iodoacetate <153>) <153>

SUBUNITS
SU	#1,8,14,15,23,24,30,72,79,84,97,102,103,125,130,148,150,152,157# ? (#8#
	x * 42000, SDS-PAGE <14>; #72# x * 28000, SDS-PAGE <2>; #1,8,79,130# x
	* 40000, SDS-PAGE <11,44,52,227>; #23# x * 96000, SDS-PAGE <128>; #84#
	x * 30000, SDS-PAGE <226>; #157# x * 85000, SDS-PAGE <283>; #14# x *
	37500, SDS-PAGE <81>; #24# x * 31997, amino acid sequence calculation
	<106>; #97# x * 37443, ADH1, calculated from sequence <172>; #15# x *
	37983, ADH3, calculated from sequence <172>; #30# x * 41300, SDS-PAGE
	<181>; #125# x * 31000, recombinant His6-tagged enzyme, SDS-PAGE <231>;
	#150# x * 36411, calculated, x * 37000, SDS-PAGE <244>; #102# x *
	37066, calculated <177>; #103# x * 37311, calculated <177>; #148# x *
	96000, wild-type, SDS-PAGE <241>; #152# x * 40000, SDS-PAGE, x * 39900,
	calculated <272>; #157# x * 88000, calculated from sequence <283>)
	<2,11,14,44,52,81,106,128,172,177,181,226,227,231,241,244,272,283>
SU	#113# octamer (#113# 8 * 45000, SDS-PAGE, 8 * 41664, calculated <215>)
	<215>
SU	#3,4,5,8,9,10,12,16,18,19,20,21,25,35,40,41,43,44,45,52,60,66,67,68,71
	74,77,78,80,87,99,148# dimer (#16# 2 * 45000, SDS-PAGE <79>; #25,77# 2
	* 28000, SDS-PAGE <61,188>; #66,80# 2 * 58000, SDS-PAGE <77,78>; #18# 2
	* 35000, SDS-PAGE <75>; #43# 2 * 38000, SDS-PAGE <114>; #8,10,35,52,78#
	2 * 40000, SDS-PAGE <16,23,24,59,87,95>; #35# 2 * 41000, SDS-PAGE <47>;
	#67# 2 * 42000, SDS-PAGE <69>; #44# 2 * 46000, SDS-PAGE <6>; #87# 2 *
	43000, SDS-PAGE <118>; #12# 2 * 36000, SDS-PAGE <45>; #21,45# 2 *
	37000, SDS-PAGE <66,70,72,165>; #41# 2 * 38000, enzyme form ADHII,
	SDS-PAGE <68>; #8# 2 * 41000, class III isoenzyme chi ADH, SDS-PAGE
	<16>; #9# 2 * 43000, ADH-1, SDS-PAGE <49>; #8# 2 * 42000, anodic enzyme
	form, SDS-PAGE <18>; #68# 2 * 42000, enzyme form ADH-2 and ADH-3,
	SDS-PAGE <60>; #5# 2 * 47000, isoenzyme C2, SDS-PAGE <48>; #5# 2 *
	39000, isoenzyme B2, SDS-PAGE <48>; #9# 2 * 40000, ADH-3, SDS-PAGE
	<49>; #9# 2 * 39000, ADH-2, SDS-PAGE <49>; #12# 2 * 41700, enzyme form
	CM-I: a polypeptide chain + C polypeptide chain, enzyme form CM-II:
	B-chain + C-chain, enzyme form CM III, homodimer of C chains, SDS-PAGE
	<46>; #5# 2 * 43000, isoenzyme A2, SDS-PAGE <48>; #41# 2 * 40000,
	enzyme form ADHI <68>; #4,71,74# 2 * 27800, SDS-PAGE <64>; #41# 2 *
	34700, enzyme form ADH-I, SDS-PAGE <67>; #3# 2 * 30000 <4>; #41# 2 *
	31100, enzyme form ADH-II, SDS-PAGE <67>; #60# 2 * 31000, ADH II,
	SDS-PAGE <113>; #45# dimer of dimers, X-ray crystallography <161>; #99#
	2 * 36900, SDS-PAGE <171>; #43# 2 * 38000, recombinant enzyme, SDS-PAGE
	<232>; #148# 2 * 48600, alcohol dehydrogenase domain, SDS-PAGE. Unlike
	the native ADHE, the alcohol dehydrogenase domain alone does not
	assemble into spirosome structures <241>; #20# 2 * 40700, calculated
	<284>)
	<4,6,16,18,21,23,24,45,46,47,48,49,59,60,61,64,66,67,68,69,70,71,72,75
	77,78,79,87,95,113,114,118,161,165,171,188,194,205,232,241,284>
SU	#45,94,104,110,121,128,131# homotetramer (#131# 4 * 40000, SDS-PAGE
	<239>; #121# 4 * 38000, SDS-PAGE <217>; #45# x-ray crystallography
	<161>; #45,94# 4 * 35000, gel filtration <159>; #45# 4 * 37585,
	electrospray mass spectrometry <154>; #110# 4 * 36000, Ta1316 ADH,
	SDS-PAGE <213>; #110# 4 * 36010, Ta1316 ADH, calculated from amino acid
	sequence <213>; #121# 4 * 37477, calculeted from sequence <217>; #128#
	4 * 38000, calculated from sequence <230>; #131# 4 * 39570, calculated
	from sequence <239>) <154,159,161,213,217,220,230,239>
SU	#46,56,57,96,142,149# monomer (#56# 1 * 45000, SDS-PAGE <147>; #46# 1 *
	39000, SDS-PAGE <149>; #142# 1 * 32000, SDS-PAGE <138>; #96# 1 * 31000,
	SDS-PAGE <168>; #57# 1 * 24600, SDS-PAGE <147>; #149# 1 * 31000,
	SDS-PAGE, 1 * 31464, calculated <243>) <138,147,149,168,243>
SU	#47,127# homodimer (#127# 2 * 28900, SDS-PAGE <225>; #47# 2 *
	42200-43000, recombinant His-tagged enzyme, SDS-PAGE <223>) <223,225>
SU	#54# decamer (#54# 10 * 43000, SDS-PAGE <99>) <99>
SU	#6,10,13,37,45,50,51,69,70,86,91,92,118,122,123,132,135,136,137,138
	154# tetramer (#69# 4 * 42000, SDS-PAGE <84>; #51# 4 * 45000, SDS-PAGE
	<82>; #92# 4 * 26000, SDS-PAGE <137>; #91# 4 * 40000, SDS-PAGE <144>;
	#122# 4 * 30000, SDS-PAGE <219>; #118# 4 * 37000, SDS-PAGE <256>; #37#
	4 * 38000, SDS-PAGE <85>; #135,136,137# 4 * 48000, SDS-PAGE <252>;
	#138# 4 * 49000, SDS-PAGE <252>; #123# 4 * 29000, SDS-PAGE <218>; #50#
	4 * 96000, SDS-PAGE <279>; #45# x-ray crystallography <157,164>; #86#
	the monomer consista of a catalytic and a cofactor-binding domain, the
	cofactor is bound between 2 domains in a cleft <127>; #45# 4 * 37588,
	calculated from amino acid sequence <163>; #45# 4 * 37591, electrospray
	mass spectrometry <163>; #45# crosslinking of ADH with
	dimethylsuberimidate and ethylene glycol bis [succinimidylsuccinate]
	produces mainly dimers and tetramers, suggesting a dimer of dimers
	assembly <163>; #6# 4 * 26961, calculated from sequence <169>; #123# 4
	* 27024, ESI-MS analysis <218>; #122# 4 * 28978, calculated from
	sequence <219>; #132# 4 * 37600, SDS-PAGE <237>; #123# 4 * 28978,
	calculated, 4 * 30000, SDS-PAGE <219>; #154# 4 * 36000, SDS-PAGE, 4 *
	35971, calculated <271>)
	<82,84,85,112,127,137,144,157,163,164,169,205,218,219,237,252,256,271
	279>
SU	#60# trimer (#60# 3 * 42000, ADH I, SDS-PAGE <113>) <113>
SU	#8,26,47,123# More (#26# quaternary organization and stability,
	overview <129>; #8# structure modelling <115>; #47# Adh3 forms a
	Ni2+-containing homodimer in its active form, crystal structure
	analysis, larger aggregates are inactive <223>; #123# tetramer
	structure results from chemical crosslinking experiments <219>)
	<115,129,219,223>
SU	#98# dodecamer (#98# 12 * 35000, SDS-PAGE <173>) <173>

PI_VALUE
PI	#102# 6.1 (#102# calculated <177>) <177>
PI	#103# 5.7 (#103# calculated <177>) <177>
PI	#110# 5.5 (#110# Ta1316 ADH, calculated from amino acid sequence <213>)
	<213>
PI	#118# 4.9 (#118# isoelectric focusing <256>) <256>
PI	#15# 8.3 (#15# calculated from sequence <172>) <172>
PI	#154# 4.8 (#154# isoelectric focusing <271>) <271>
PI	#154# 5.1 (#154# calculated <271>) <271>
PI	#157# 6.98 (#157# calculated from sequence <283>) <283>
PI	#47# 5.23 (#47# sequence calculation <223>) <223>
PI	#87# 6 <118>
PI	#97# 6.3 (#97# calculated from sequence, ADH1 <172>) <172>

APPLICATION
AP	#13# biotechnology (#13# possible usage of the enzyme in bioindustrial
	processes and as biosensor <126>) <126>
AP	#133,134,143# degradation (#143# direct conversion of switchgrass to
	ethanol without conventional pretreatment of the biomass is
	accomplished by deletion of lactate dehydrogenase and heterologous
	expression of a Clostridium thermocellum bifunctional
	acetaldehyde/alcohol dehydrogenase in Caldicellulosiruptor bescii.
	Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make
	ethanol, 70% of the fermentation products in the engineered strain are
	ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with
	decreased production of acetate by 38% compared with wild-type <267>;
	#133# expression of AdhB gene in an ldh deletion mutant of
	Caldicellulosiruptor bescii leads to ethanol production at 75°C, near
	the ethanol boiling point. The AdhB expressing strain produces ethanol
	(1.4 mM on Avicel, 0.4 mM on switchgrass) as well as acetate (13.0 mM
	on Avicel, 15.7 mM on switchgrass). The addition of 40 mM MOPS to the
	growth medium increases the maximal growth yield of C. bescii by
	approximately twofold <249>; #134# expression of AdhB gene in an ldh
	deletion mutant of Caldicellulosiruptor bescii leads to ethanol
	production at 75°C, near the ethanol boiling point. The AdhE
	expressing strain produce ethanol (2.3 mM on Avicel, 1.6 mM on
	switchgrass) and acetate (12.3 mM on Avicel, 15.1 mM on switchgrass).
	The addition of 40 mM MOPS to the growth medium increases the maximal
	growth yield of C. bescii by approximately twofold <249>) <249,267>
AP	#155,156# biofuel production (#155# ethanol production by the
	hyperthermophilic archaeon Pyrococcus furiosus by expression of
	bacterial bifunctional alcohol dehydrogenase (Tx-AdhE). Ethanol and
	acetate are the only major carbon end-products from glucose under these
	conditions. The amount of ethanol produced per estimated glucose
	consumed is increased from the background level 0.7 respectively.
	Although ethanol production from acetyl-CoA is demonstrated in
	Pyrococcus furiosus, the highest ethanol yield (from strain Te-AdhEA)
	is still lower than that of the AAA pathway in Pyrococcus furiosus,
	which functions via the native enzymes acetyl-CoA synthetase (ACS) and
	aldehyde oxidoreductase (AOR) along with heterologously expressed
	alcohol dehydrogenase (AdhA) <281>; #156# expression in Pyrococcus
	furiosus from which the native aldehyde oxidoreductase (AOR) gene is
	deleted supports ethanol production. The highest amount of ethanol
	(estimated 61% theoretical yield) is produced when adhE and adhA from
	Thermoanaerobacter are co-expressed. A strain containing the
	Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is
	constructed. The AdhA gene is amplified from Thermoanaerobacter sp.
	X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514
	is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of
	the bacterial strains expressing the various heterologous AdhE genes,
	only those containing AdhE and AdhA from Thermoanaerobacter sp.
	produced ethanol above background. The Thermoanaerobacter ethanolicus
	AdhEA strain containing both AdhE and AdhA produces the most ethanol
	(4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6
	mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and
	Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate
	are the only major carbon end-products from glucose under these
	conditions. For these four strains, the amount of ethanol produced per
	estimated glucose consumed is increased from the background level to
	1.2, 1.0, 0.8 and 0.7 respectively <281>) <281>
AP	#6,10,13,15,28,29,34,36,39,41,43,88,92,118,123,139,140,143,144,145,147
	151,152# synthesis (#43# enzyme can be used in preparative scale
	enantioselective oxidation of sec-alcohol in asymmetric reduction of
	ketones, using acetone and 2-propanol, respectively, as cosubstrates
	for cofactor-regeneration via a coupled-substrate approach <114>; #28#
	production of (3R,5S)-6-benzyloxy-3,5-dihydroxy-hexanoic acid ethyl
	ester, which is a key chiral intermediate for anticholesterol drugs
	that act by inhibition of hydroxy methyl glutaryl coenzyme A reductase
	<133>; #15# production of
	(4S,6S)-5,6-dihydro-4-hydroxy-6-methyl-4H-thieno[2,3b]thiopyran-7
	7dioxide, which is an intermediate in the synthesis of the carbonic
	anhydrase inhibitor trusopt. Trusopt is a novel, topically active
	treatment for glaucoma <134>; #39# production of
	(S)-1-Phenyl-2-propanol, which is used as an intermediate for the
	synthesis of amphetamines and as a precursor for anti-hypertensive
	agents and spasmolytics or anti-epileptics <131>; #88# production of
	(S)-4-(3,4-methylenedioxyphenyl)-2-propanol, which is converted to
	LY300164, an orally active benzodiazepine <132>; #92# LSADH catalyzed
	the enantioselective reduction of some ketones with high enantiomeric
	excesses: phenyl trifluoromethyl ketone to (S)-1-phenyltrifluoroethanol
	(>99% e.e.), acetophenone to (R)-1-phenylethanol (99% e.e.), and
	2-heptanone to (R)-2-heptanol (>99% e.e.) in the presence of 2-propanol
	without an additional NADH regeneration system. Therefore, it would be
	a useful biocatalyst <137>; #10# the photochemical and enzymatic
	synthesis of methanol from formaldehyde with alcohol dehydrogenase and
	NAD+ photoreduction by the visible-light photosensitization of zinc
	tetraphenylporphyrin tetrasulfonate in the presence of methylviologen,
	diaphorase, and triethanolamine is developed <187>; #43# alcohol
	dehydrogenases represent an important group of biocatalysts due to
	their ability to stereospecifically reduce prochiral carbonyl compounds
	<232>; #41# alpha-ketoisovalerate decarboxylase Kivd from Lactococcus
	lactis combined with alcohol dehydrogenase Adh3 from Zymomonas mobilis
	are the optimum candidates for 3-methyl-1-butanol production in
	Corynebacterium glutamicum. The recombinant strain produces 0.182 g/l
	of 3-methyl-1-butanol and 0.144 g/l of isobutanol after 12 h of
	incubation. Further inactivation of the E1 subunit of pyruvate
	dehydrogenase complex gene (aceE) and lactic dehydrogenase gene (ldh)
	improves the 3-methyl-1-butanol titer to 0.497 g/l after 12 h of
	incubation <263>; #147# construction of a synthetic pathway for
	bioalcohol production at 70°C by insertion of the gene for alcohol
	dehydrogenase AdhA into the archaeon Pyrococcus furiosus. The
	engineered strain converts glucose to ethanol via acetate and
	acetaldehyde, catalyzed by the host-encoded aldehyde ferredoxin
	oxidoreductase AOR and heterologously expressed AdhA, in an
	energy-conserving, redox-balanced pathway. The AOR/AdhA pathway also
	converts exogenously added aliphatic and aromatic carboxylic acids to
	the corresponding alcohol using glucose, pyruvate, and/or hydrogen as
	the source of reductant. By heterologous coexpression of a
	membrane-bound carbon monoxide dehydrogenase, CO is used as a reductant
	for converting carboxylic acids to alcohols <266>; #139# construction
	of an enzyme-immobilized bioanode that can operate at high
	temperatures. The catalytic current for ethanol oxidation at Ru
	complex-modified electrodes increases at 80°C up to 12fold compared
	with room temperature <254>; #143# deletion of the hypoxanthine
	phosphoribosyltransferase gene in ethanol tolerant strain adhE*(EA),
	carrrying mutation P704L/H734R in the alcohol dehydrogenase gene, and
	deletion of lactate dehydrogenase (ldh) to redirect carbon flux towards
	ethanol reults in a strain producing 30% more ethanol than wild type on
	minimal medium. The engineered strain retains tolerance to 5% v/v
	ethanol, resulting in an ethanol tolerant platform strain <264>; #34#
	engineering of a strain of Corynebacterium glutamicum, based on
	inactivation of the pyruvate dehydrogenase complex, pyruvate:quinone
	oxidoreductase, transaminase B, and additional overexpression of the
	IlvBNCD genes, encoding acetohydroxyacid synthase, acetohydroxyacid
	isomeroreductase, and dihydroxyacid dehydratase, for the production of
	isobutanol from glucose under oxygen deprivation conditions by
	inactivation of L-lactate and malate dehydrogenases, implementation of
	ketoacid decarboxylase from Lactococcus lactis, alcohol dehydrogenase 2
	(ADH2) from Saccharomyces cerevisiae, and expression of the pntAB
	transhydrogenase genes from Escherichia coli. The resulting strain
	produces isobutanol with a substrate-specific yield (YP/S) of 0.60 mol
	per mol of glucose. Chromosomally encoded alcohol dehydrogenase AdhA
	rather than the plasmid-encoded ADH2 from Saccharomyces cerevisiae is
	involved in isobutanol formation, and overexpression of the
	corresponding AdhA gene increases the YP/S to 0.77 mol of isobutanol
	per mol of glucose. Inactivation of the malic enzyme significantly
	reduces the YP/S, indicating that the metabolic cycle consisting of
	pyruvate and/or phosphoenolpyruvate carboxylase, malate dehydrogenase,
	and malic enzyme is responsible for the conversion of NADH + H+ to
	NADPH + H+. In fed-batch fermentations with an aerobic growth phase and
	an oxygen-depleted production phase, the most promising strain produces
	about 175 mM isobutanol, with a volumetric productivity of 4.4 mM per
	h, and shows an overall YP/S of about 0.48 mol per mol of glucose in
	the production phase <242>; #144# engineering of Klebsiella pneumoniae
	to produce 2-butanol from crude glycerol as a sole carbon source by
	expressing acetolactate synthase (IlvH), keto-acid reducto-isomerase
	(IlvC) and dihydroxyacid dehydratase (IlvD) from Klebsiella pneumoniae,
	and alpha-oxoisovalerate decarboxylase (Kivd) and alcohol dehydrogenase
	(AdhA) from Lactococcus lactis. The engineered strain produce 2-butanol
	(160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol
	pathway by inactivating alpha-acetolactate decarboxylase (Adc) further
	improves the yield of 2-butanol from 160 to 320 mg/l <250>; #140#
	enhancement of ethanol production capacity of Clostridium thermocellum
	by transferring pyruvate decarboxylase and alcohol dehydrogenase genes
	of the homoethanol pathway from Zymomonas mobilis. Both transferring
	pyruvate decarboxylase and alcohol dehydrogenase are functional in
	Clostridium thermocellum, but the presence of and alcohol dehydrogenase
	severely limits the growth of the recombinant strains, irrespective of
	the presence or absence of the pyruvate decarboxylase gene. The
	recombinant strain shows two-fold increase in pyruvate carboxylase
	activity and ethanol production when compared with the wild type strain
	<253>; #123# enzyme catalyses the reduction of alpha-methyl and
	alpha-ethyl benzoylformate, and methyl o-chlorobenzoylformate with 100%
	conversion to methyl (S)-mandelate [17% enantiomeric excess (ee)],
	ethyl (R)-mandelate (50% ee), and methyl (R)-o-chloromandelate (72%
	ee), respectively, with an efficient in situ NADH-recycling system
	which involves glucose and a thermophilic glucose dehydrogenase <219>;
	#6# enzyme catalyzes the following reactions with Prelog specificity:
	the reduction of acetophenone, 2,2,2-trifluoroacetophenone,
	alpha-tetralone, and alpha-methyl and alpha-ethyl benzoylformates to
	(S)-1-phenylethanol (>99% enantiomeric excess),
	(R)-alpha-(trifluoromethyl)benzyl alcohol (93% enantiomeric excess),
	(S)-alpha-tetralol (>99% enantiomeric excess), methyl (R)-mandelate
	(92% enantiomeric excess), and ethyl (R)-mandelate (95% enantiomeric
	excess), respectively, by way of an efficient in situ NADH-recycling
	system involving 2-propanol and a second thermophilic ADH <169>; #43#
	expression of enzyme in auxotrophic Arxula adeninivorans, Hansenula
	polymorpha, and Saccharomyces cerevisiae strains using yeast ribosomal
	DNA integrative expression cassettes. Recombinant ADH accumulates
	intracellularly in all strains tested. The best yields of active enzyme
	are obtained from A. adeninivorans, with Saccharomyces cerevisiae
	producing intermediate amounts. Although Hansenula polymorpha is the
	least efficient producer overall, the product obtained is most similar
	to the enzyme synthesized by Rhodococcus ruber 219 with respect to its
	thermostability <232>; #140# expression of pyruvate decarboxylase and
	alcohol dehydrogenase in Clostridium thermocellum DSM 1313. Though both
	enzymes are functional in Clostridium thermocellum, the presence of
	alcohol dehydrogenase severely limits the growth of the recombinant
	strains, irrespective of the presence or absence of the pyruvate
	decarboxylase gene <253>; #10# in order to increase production of
	isobutanol, 2-oxoacid decarboxylase (KDC) and alcohol dehydrogenase
	(ADH) are expressed in Saccharomyces cerevisiae to enhance the
	endogenous activity of the Ehrlich pathway. Overexpression Ilv2, which
	catalyzes the first step in the valine synthetic pathway, and deletion
	of the PDC1 gene encoding a major pyruvate decarboxylase alters the
	abundant ethanol flux via pyruvate. Along with modification of culture
	conditions, the isobutanol titer is elevated 13fold, from 11 mg/l to
	143 mg/l, and the yield is 6.6 mg/g glucose <261>; #145# overexpression
	of the adhB gene results in a significant increase in the ethanol level
	<262>; #13# protocol for the synthesis of [4R-(2)H]NADH with high yield
	by enzymatic oxidation of 2-propanol-d(8) <269>; #36# recombinant
	enzyme activity can be improved by coexpression of archaeal chaperones
	(i.e., gamma-prefoldin and thermosome). Ricinoleic acid
	biotransformation activity of recombinant Escherichia coli expressing
	Micrococcus luteus alcohol dehydrogenase and the Pseudomonas putida
	KT2440 Baeyer-Villiger monooxygenase improves significantly with
	coexpression of gamma-prefoldin or recombinant themosome originating
	from the deep-sea hyperthermophile archaea Methanocaldococcus
	jannaschii. The degree of enhanced activity is dependent on the
	expression levels of the chaperones <248>; #118# semi-preparative
	biocatalysis at 60°C using the stabilized mutant C257L, employing
	butyraldehyde for in situ cofactor regeneration with only catalytic
	amounts of NAD+, yields up to 23% conversion of omega-hydroxy lauric
	acid methyl ester to omega-oxo lauric acid methyl ester after 30 min
	<246>; #10# simplified production scheme for isobutanol based on a
	cell-free immobilized enzyme system. Immobilized enzymes keto-acid
	decarboxylase (KdcA) and alcohol dehydrogenase (ADH) plus formate
	dehydrogenase (FDH) for NADH recycle in solution produce isobutanol
	titers 8 to 20 times higher than the highest reported titers with
	Saccharomyces cerevisiae on a mol/mol basis. Conversion rates and low
	protein leaching are achieved by covalent immobilization on
	methacrylate resin. The enzyme system without in situ removal of
	isobutanol achieves a 55% conversion of ketoisovaleric acid to
	isobutanol at a concentration of 0.135 mol isobutanol produced for each
	mol ketoisovaleric acid consumed <251>; #13# synthesis of the cinnamyl
	alcohol by means of enzymatic reduction of cinnamaldehyde using alcohol
	both as an isolated enzyme, and in recombinant Escherichia coli whole
	cells in an efficient and sustainable one-phase system. The reduction
	of cinnamaldehyde (0.5 g/l, 3.8 mmol/l) by the isolated enzyme occurrs
	in 3 h at 50°C with 97% conversion, and yields high purity cinnamyl
	alcohol (98%) with a yield of 88% and a productivity of 50 g/g enzyme.
	The reduction of 12.5 g/l (94 mmol/l) cinnamaldehyde by whole cells in
	6 h, at 37°C and no requirement of external cofactor occurrs with 97%
	conversion, 82% yield of 98% pure alcohol and a productivity of 34 mg/g
	wet cell weight <234>; #151# synthetic pathway for n-butanol production
	from acetyl coenzyme at 70°C, using beta-ketothiolase Thl,
	3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA
	dehydratase Crt from Caldanaerobacter subterraneus subsp.
	tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta
	thermophila and bifunctional aldehyde dehydrogenase AdhE and and
	butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but
	with different amounts of ethanol as a coproduct, because of the broad
	substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics
	model, validated via comparison to in vitro experiments, is used to
	determine relative enzyme ratios needed to maximize n-butanol
	production. By using large relative amounts of Thl and Hbd and small
	amounts of Bad and Bdh, >70% conversion to n-butanol is observed in
	vitro, but with a 60% decrease in the predicted pathway flux <245>;
	#10# yeast alcohol dehydrogenase with its cofactor NAD+ can be stably
	encapsulated in liposomes composed of
	1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The liposomes are 100
	nm in mean diameter, the liposomal ADH and NAD+ concentrations are 2.3
	mg/ml and 3.9 mM, respectively. Free ADH is increasingly deactivated
	during its incubation at 45°C for 2 h with decrease of the enzyme
	concentration from 3.3 to 0.01 mg/ml because of the dissociation of
	tetrameric ADH into its subunits. Both liposomal enzyme systems, in
	presence and absence of NAD+, show stabilities at both 45 and 50°C
	much higher than those of the free enzyme systems, implying that the
	liposome membranes stabilize the enzyme tertiary and quaternary
	structures. The enzyme activity of the liposomes in presence of NAD+
	show a stability higher than that in absence of NAD+ with a more
	remarkable effect of NAD+ at 50°C than at 45°C <179>; #29#
	immobilization of enzyme on metal-derivatized epoxy Sepabeads. The
	highest immobilization efficiency (100%) and retention activity (60%)
	are achieved after 48 h of incubation of the enzyme with Niepoxy
	Sepabeads support in 100 mM Tris-HCl buffer, pH 8, containing 3 M KCl
	at 5°C. A significant increase in the stability of the immobilized
	enzyme is achieved by blocking the unreacted epoxy groups with
	ethylamine. The immobilization process increases the enzyme stability,
	thermal activity, and organic solvents. One step
	purification-immobilization can be carried out on metal chelate-epoxy
	Sepabeads <240>; #152# under optimized conditions, the enzyme produces
	600 mg all-trans-retinol per l after 3 h, with a conversion yield of
	27.3% (w/w) and a productivity of 200 mg per l and h <272>)
	<114,131,132,133,134,137,169,179,187,219,232,234,240,242,245,246,248
	250,251,253,254,261,262,263,264,266,269,272>
AP	#8,23# medicine (#23# isozyme ADH2 is a target for anti-amoebic agents
	<123>; #8# organ simulations indicate that higher therapeutic
	acetaminophen (0.5 mM) inhibits 16% of allotype ADH1B*1/*1 hepatic ADH
	activity at 2-20 mM ethanol and that therapeutic salicylate (1.5 mM)
	inhibits 30-31% of the allotype ADH1B*2/*2 activity, suggesting
	potential significant inhibitions of ethanol first-pass metabolism in
	these allelotypes <273>) <123,273>

ENGINEERING
EN	#10# H47R (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# M294L (#10# 7-10fold increase in reactivity, V/Km, with butanol,
	pentanol and hexanol <91>; #10# increased activity compared to the
	wild-type enzyme <120>) <91,120>
EN	#10# T48A (#10# inactive mutant <120>) <120>
EN	#10# W57M (#10# slightly reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# W57L (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# W93A (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# D49N (#10# highly reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# E68Q (#10# highly reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# T48S (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# T48S/T93A (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# T48S/W57M/W93A (#10# reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# T48C (#10# inactive mutant <120>) <120>
EN	#10# H51E (#10# highly reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# S198F (#10# highly reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# G224I (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# G225R (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# D223G (#10# highly reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# D223G/G225R (#10# nearly inactive mutant <120>) <120>
EN	#10# L203A (#10# reduced activity compared to the wild-type enzyme
	<120>) <120>
EN	#10# L203A/T178S (#10# reduced activity compared to the wild-type
	enzyme <120>) <120>
EN	#10# G204A (#10# nearly inactive mutant <120>) <120>
EN	#10# DELTAA200/A201L (#10# highly reduced activity compared to the
	wild-type enzyme <120>) <120>
EN	#10# S269I (#10# nearly inactive mutant <120>) <120>
EN	#10# Y295C (#10# mutant is able to catalyze the NADH-dependent
	reduction of 5-hydroxymethylfurfural, an inhibitor of yeast
	fermentation <282>) <282>
EN	#10# S110P/Y295C (#10# mutant is able to catalyze the NADH-dependent
	reduction of 5-hydroxymethylfurfural, an inhibitor of yeast
	fermentation, best activity among the mutants isolated <282>) <282>
EN	#10,40# H51Q (#10# reduced activity compared to the wild-type enzyme
	<120>; #40# site-directed mutagenesis, shifting of pH dependency,
	increased activity at pH 8.0, decrease of the rate of isomerization of
	the enzyme-NAD+ complex, which becomes the limiting step for ethanol
	oxidation <111>) <111,120>
EN	#104# W95L (#104# the mutant displays no apparent activity with
	short-chain primary and secondary alcohols and poor activity with
	aromatic substrates and coenzyme, the substitution affects the
	structural stability of the archaeal ADH, decreasing its thermal
	stability without relevant changes in secondary structure, optimum pH
	is at about pH 10 <207>) <207>
EN	#104# W95L/N249Y (#104# the mutant exhibits higher activity but
	decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+
	and NADH compared to the wild type enzyme, optimum pH is at about pH
	8.6 <207>) <207>
EN	#118# V260A (#118# kinetic parameters and temperature dependencies
	similar to wild-type <257>) <257>
EN	#118# Y25A (#118# kinetic parameters and temperature dependencies
	similar to wild-type <257>; #118# mutation in the dimer-dimer
	interface, results in kinetic behavior similar to that of mutantion
	W87A <260>) <257,260>
EN	#118# W87A (#118# mutation results in a loss of the Arrhenius break
	seen at 30°C for the wild-type enzyme and an increase in cold lability
	due to destabilization of the active tetrameric form. Kinetic isotope
	effects are nearly temperature-independent over the experimental
	temperature range, and similar in magnitude to those measured above
	30°C for the wild-type enzyme <260>) <260>
EN	#118# W87F (#118# investigation on protein dynamics on the microsecond
	time scale. Mutant exhibits a fast, temperature-independent microsecond
	decrease in fluorescence followed by a slower full recovery of the
	initial fluorescence. The results rule out an ionizing histidine as the
	origin of the fluorescence quenching. A Trp49-containing dimer
	interface may act as a conduit for thermally activated structural
	change within the protein interior <258>) <258>
EN	#118# C257L (#118# mutation introduced to improve stability under
	oxidzing conditions. Mutant exhibits prolonged stability and an
	elevated inactivation temperature <246>) <246>
EN	#118# W49F/W167Y (#118# kinetic parameters and temperature dependencies
	similar to wild-type <257>) <257>
EN	#118# Y25A/W49F/W167Y (#118# kinetic parameters and temperature
	dependencies similar to wild-type <257>) <257>
EN	#118# W49F/W167Y/V260A (#118# kinetic parameters and temperature
	dependencies similar to wild-type <257>) <257>
EN	#118# Y25A/W49F/W167Y/V260A (#118# kinetic parameters and temperature
	dependencies similar to wild-type <257>) <257>
EN	#118# W49F/W87F (#118# kinetic parameters and temperature dependencies
	similar to wild-type <257>) <257>
EN	#118# Y25A/W49F/W87F (#118# kinetic parameters and temperature
	dependencies similar to wild-type <257>) <257>
EN	#118# W49F/W87F/V260A (#118# kinetic parameters and temperature
	dependencies similar to wild-type <257>) <257>
EN	#118# Y25A/W49F/W87F/V260A (#118# kinetic parameters and temperature
	dependencies similar to wild-type <257>) <257>
EN	#118# W87F/H43A (#118# investigation on protein dynamics on the
	microsecond time scale. Mutant exhibits a fast, temperature-independent
	microsecond decrease in fluorescence followed by a slower full recovery
	of the initial fluorescence. The results rule out an ionizing histidine
	as the origin of the fluorescence quenching. A Trp49-containing dimer
	interface may act as a conduit for thermally activated structural
	change within the protein interior <258>) <258>
EN	#118,126,142,148,156# more (#126# generation of the ADH3 deletion
	mutant, complementation of the HpADH3 mutant by an HpADH3 expression
	cassette fused to a strong constitutive promoter, the resulting strain
	produced a significantly increased amount of ethanol compared to the
	wild-type strain in a glucose medium, while in a xylose medium, the
	ethanol production is dramatically reduced in an HpADH3 overproduction
	strain compared to that in the wild-type strain, phenotype analysis of
	DELTAHpADH3 and DELTAHpADH1/DELTAHpADH3 mutants, overview <222>; #148#
	expression of alcohol dehydrogenase domain alone, a minimal functional
	unit corresponds to amino acids 459-869 <241>; #118# mutations Y25A (at
	the dimer interface) and V260A (at the cofactor-binding domain) exhibit
	opposing low-temperature effects on the hydride tunneling step. The
	distal Y25A increases active-site flexibility, V260A introduces a
	temperature-dependent equilibration process, and the double mutant
	(Y25A/V260A) eliminates the temperature-dependent transition sensed by
	the active-site tryptophan in the presence of V260A. V260A displays a
	structural change in the active-site environment/solvation <257>; #142#
	replacement of three mobile loops positioned at the top of the
	canonical (alpha/beta)8-barrel structure by those from human aldose
	reductase. Replacement of Loops A and B is sufficient to impart from
	human aldose reductase activity into AdhD, and the resulting chimera
	retains the thermostability of the parent enzyme. No active chimeras
	are observed when the from human aldose reductase loops are grafted
	into a previously engineered cofactor specificity mutant of AdhD, which
	displays similar kinetics to from human aldose reductase with the model
	substrate DL-glyceraldehyde <268>; #156# expression of a mutant enzyme
	(with a glycine to aspartic acid mutation in the NADH binding site of
	the ADH domain of AdhE) in Pyrococcus furiosus from with the native
	aldehyde oxidoreductase (AOR) gene is deleted results in a reduced
	ethanol production to the background level <281>) <222,241,257,268,281>
EN	#141# A25Y (#141# mutation in the dimer-dimer interface, leads to a
	more thermostable enzyme and a change in the rate-determining step at
	low temperature <260>) <260>
EN	#143# P704L/H734R (#143# mutation leads to ethanol-tolerant phenotype.
	P704L may affect cofactor-binding directly, while mutation H734R is
	close to the active site iron atom. Mutant displays a complete loss of
	NADH-dependent activity with concomitant acquisition of NADPH-dependent
	activity <265>) <265>
EN	#40# W54L (#40# less active than the wild-type enzyme with ethanol,
	1-propanol and 1-butanol. With 1-pentanol and 1-hexanol the mutant
	enzyme is a better catalyst than the wild-type enzyme <92>) <92>
EN	#40# H51Q/K228R (#40# site-directed mutagenesis, kinetic effects <111>)
	<111>
EN	#45# N249Y (#45# mutant exhibits increased catalytic activity compared
	to the wild type enzyme <157>; #45# mutant shows increased thermal
	stability and increased catalytic activity compared to the wild type
	enzyme <154>; #45# shows 7fold higher specific activity compared to the
	wild type enzyme, is active up to 95°C and more stable than the native
	enzyme, has acquired an improved resistance to proteolysis by
	thermolysin and shows a decreased activating effect by treatment with
	denaturants at moderate concentration <163>) <154,157,163>
EN	#45# E97C (#45# shows the same activity but a reduced thermostability
	with respect to the wild type recombinant protein <165>) <165>
EN	#5# P47H (#5# site-directed mutagenesis, about 100fold increased
	activity compared to the wild-type enzyme <110>) <110>
EN	#5# P47A (#5# site-directed mutagenesis, about 100fold increased
	activity compared to the wild-type enzyme <110>) <110>
EN	#5# P47Q (#5# site-directed mutagenesis, about 100fold increased
	activity compared to the wild-type enzyme <110>) <110>
EN	#8# A93F (#8# isozyme alphaalpha, altered active site structure and
	inhibitor binding <109>) <109>
EN	#8# S48T (#8# isozyme gamma(2)gamma(2), altered active site structure
	and inhibitor binding <109>) <109>
EN	#8# V141L (#8# isozyme gamma(2)gamma(2), altered active site structure
	and inhibitor binding <109>) <109>
EN	#83# G223D (#83# unaltered cofactor specificity compared to the
	wild-type enzyme <125>) <125>
EN	#83# T224I (#83# unaltered cofactor specificity compared to the
	wild-type enzyme <125>) <125>
EN	#83# H225N (#83# unaltered cofactor specificity compared to the
	wild-type enzyme <125>) <125>
EN	#83# G223D/T224I/H225N (#83# altered cofactor specificity, highly
	reduced activity with NADP+ compared to the wild-type enzyme,
	wild-type-like activity with NAD+ <125>) <125>
EN	#83# G223D/T224I (#83# highly reduced activity with NADP+ compared to
	the wild-type enzyme, wild-type-like activity with NAD+ <125>) <125>

CLONED
CL	#5# (class III enzyme) <9>
CL	#5# (expression of isozymes in Escherichia coli strain BL21) <119>
CL	#6# (overexpressed in Escherichia coli) <169>
CL	#8# (class IV enzyme, expression in Escherichia coli) <53>
CL	#8# (5-7 genes encoding ADH, DNA and amino acid sequence determination
	and analysis, polymorphism and allelic frequencies analysis, gene ADH2
	possesses 2 allelic forms with Ile308 or Val308, expression of ADH2
	alloenzymes in Escherichia coli) <115>
CL	#8# (expression of ADH1C*2 in Escherichia coli) <116>
CL	#8# (expression of ADH4 in Escherichia coli) <124>
CL	#8# (expression of isozymes in Escherichia coli strain BL21) <119>
CL	#8# (expression of human ADH1 in an in vitro transcription/translation
	system, N-terminally GST-tagged ADH1 in COS cells and in Escherichia
	coli) <228>
CL	#9# (expression of rat ADH5 in an in vitro transcription/translation
	system, GFP-tagged ADH5 in COS cells, but no soluble ADH5 protein from
	heterologously expression in Escherichia coli cells with expression
	systems successfully used for other mammalian ADHs, including fused to
	glutathione-S-transferase) <228>
CL	#10# <87,91,261>
CL	#10# (expressed in Escherichia coli DH5alpha cells) <202>
CL	#10# (expressed in Hep-G2 cells) <209>
CL	#10# (mutant enzyme S109P/L116S/Y294) <193>
CL	#10# (overexpression in Saccharomyces bayanus) <170>
CL	#13# (overexpression as GST-fusion protein in Escherichia coli) <126>
CL	#15# (ADH3 is expressed in recombinant Escherichia coli) <172>
CL	#20# (expression in Escherichia coli) <284>
CL	#23# (expression in Escherichia coli) <123>
CL	#24# (DNA and amino acid sequence determination and analysis,
	functional expression in Escherichia coli using a rhamnose-inducible
	system) <106>
CL	#26# (expression in Escherichia coli strain TG-1) <129>
CL	#30# (gene encoding for ADH of the haloalkaliphilic archaeon
	Natronomonas pharaonis, which has a 1,068-bp open reading frame that
	encodes a protein of 355 amino acids, is cloned into the pET28b vector
	and is expressed in Escherichia coli) <181>
CL	#32# <91>
CL	#43# (DNA and amino acid sequence determination and analysis,
	expression of His-tagged enzyme under the control of the strong
	constitutive Arxula adeninivorans-derived TEF1 promoter in auxotrophic
	Arxula adeninivorans strain G1214, Hansenula polymorpha strain RB11,
	and Saccharomyces cerevisiae strainSEY6210, using different expression
	modules for transformation, evaluation of effeciency, overview.
	Expression in Arxula adeninivorans is most effective) <232>
CL	#45# (expressed in Escherichia coli) <157,159>
CL	#45# (expressed in Escherichia coli JM109(DE3) cells) <165>
CL	#45# (expressed in Escherichia coli RB791 cells) <154,161>
CL	#45# (expressed in Escherichia coli strain RB791) <163>
CL	#47# (gene adh3, sequence comparison, expression of N-terminally
	His-tagged enzyme in Escherichia coli strains NovaBlue Singles and
	M15[pREP4]) <223>
CL	#53# (expression in yeast) <151>
CL	#84# (gene chy1186, overexpression in Escherichia coli strain BL21
	(DE3), subcloning in Escherichia coli strain DH5alpha) <226>
CL	#91# <144>
CL	#93# (expressed in Escherichia coli BL21 Star (DE3) cells) <162>
CL	#94# (expressed in Escherichia coli) <159>
CL	#95# (expressed in Escherichia coli BL21(DE3) cells) <156>
CL	#96# <168>
CL	#97# (ADH1 is expressed in recombinant Escherichia coli) <172>
CL	#98# (expression in Escherichia coli) <173>
CL	#99# (expression in Escherichia coli) <171>
CL	#102# <177>
CL	#103# <177>
CL	#104# (expressed in Escherichia coli RB791 cells) <207>
CL	#104# (expression in Escherichia coli host strain PBL339) <235>
CL	#106# (expressed in Escherichia coli BL21(DE3) cells) <195>
CL	#109# (expressed in Escherichia coli DH5alpha cells) <210>
CL	#110# (expressed in Escherichia coli BL21 (DE3) pLysS cells) <213>
CL	#111# (expressed in Escherichia coli BL21 (DE3) cells) <197>
CL	#112# (expressed in Escherichia coli DH5alpha cells) <202>
CL	#113# (expression in Escherichia coli) <215>
CL	#114# (expression in Escherichia coli) <215>
CL	#118# <258,260>
CL	#118# (expression in Escherichia coli) <246>
CL	#121# (expression in Escherichia coli) <217>
CL	#122# (overexpressed in Escherichia coli) <219>
CL	#123# (expression in Escherichia coli) <219>
CL	#123# (heterologously overexpressed in Escherichia coli) <218>
CL	#124# (gene GmAdh2, quantitative RT-PCR expression analysis,
	phylogenetic analysis) <233>
CL	#125# (DNA and amino acid sequence determination and analysis,
	recombinant expression of His6-tagged BmADH protein in Escherichia coli
	strain BL21 (DE3)) <231>
CL	#126# (gene ADH3, subcloning in Escherichia coli strain DH5alpha,
	recombinant expression of His6-tagged enzyme in Echerichia coli strain
	BL21 (DE3), complementation of the HpADH3 mutant by an HpADH3
	expression cassette fused to a strong constitutive promoter, the
	resulting strain produced a significantly increased amount of ethanol
	compared to the wild-type strain in a glucose medium, while in a xylose
	medium, the ethanol production is dramatically reduced in an HpADH3
	overproduction strain compared to that in the wild-type strain,
	semi-quantitative RT-PCR analysis) <222>
CL	#128# (expression in Escherichia coli. The correct folding of the AdhC
	enzyme from hyperthermophilic Pyrococcus furiosus in mesophilic
	recombinant Escherichia coli is greatly influenced by the cultivation
	temperature. When grown at temperatures above the optimal growth
	temperature, Escherichia coli produces heat shock proteins to prevent
	protein aggregation. Heat shock proteins are known for their chaperonin
	activity, i.e., they help the protein folding and are responsible for
	an efficient protein quality control. When heated at 45°C for 2.5 h
	prior to induction, an increase of the activity is monitored compared
	to the standard cultivation at 37°C. The fast increase to 42°C yields
	more active enzyme than the slow increase to 42°C. This suggests that
	heat shock proteins either assist in the correct folding of the AdhC,
	or maybe even allow for resolubilization of (partially) denatured
	molecules. The cultivation at 45°C is not successful) <230>
CL	#131# (overexpressed in Escherichia coli) <236>
CL	#131# (expressed in Escherichia coli) <239>
CL	#132# (homologously expressed) <237>
CL	#133# (expression in Caldicellulosiruptor bescii) <249>
CL	#134# (expression in Caldicellulosiruptor bescii) <249>
CL	#135# (expression in Escherichia coli) <252>
CL	#136# (expression in Escherichia coli) <252>
CL	#137# (expression in Escherichia coli) <252>
CL	#138# (expression in Escherichia coli) <252>
CL	#140# (expression in Clostridium thermocellum) <253>
CL	#140# (expression in Clostridium thermocellum DSM 1313) <253>
CL	#141# (expression in Escherichia coli) <260>
CL	#142# (expression in Escherichia coli) <138>
CL	#145# <262>
CL	#147# <266>
CL	#148# <241>
CL	#149# (expression in Escherichia coli) <243>
CL	#150# (expression in Escherichia coli) <244>
CL	#151# (expression in Escherichia coli) <245>
CL	#152# (expression in Escherichia coli) <272>
CL	#153# (expression in Escherichia coli) <280>
CL	#155# (expression of Tx-AdhE in Pyrococcus furiosus from with the
	native aldehyde oxidoreductase (AOR) gene is deleted. Ethanol and
	acetate are the only major carbon end-products from glucose under these
	conditions. The amount of ethanol produced per estimated glucose
	consumed is increased from the background level 0.7 respectively) <281>
CL	#156# (expression in Pyrococcus furiosus from which the native aldehyde
	oxidoreductase (AOR) gene is deleted. A strain containing the
	Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is
	constructed. The AdhA gene is amplified from Thermoanaerobacter sp.
	X514. The amino acid sequence of TxAdhA is identical to that of TeAdhA.
	Of the bacterial strains expressing the various heterologous AdhE
	genes, only those containing AdhE and AdhA from Thermoanaerobacter sp.
	produced ethanol above background. The Te-AdhEA strain containing both
	AdhE and AdhA produces the most ethanol (4.2 mM), followed by Te-AdhE
	(2.6 mM), AdhA (1.8 mM) and Tx-AdhE (1.5 mM). Ethanol and acetate are
	the only major carbon end-products from glucose under these conditions.
	For these four strains, the amount of ethanol produced per estimated
	glucose consumed is increased from the background level to 1.2, 1.0,
	0.8 and 0.7 respectively) <281>
CL	#159# <274>
CL	#260# (expressed in Escherichia coli BL21DE3pLysS cells) <211>

CRYSTALLIZATION
CR	#8# <12>
CR	#8# (isozyme alphaalpha in complex with inhibitor
	N-cyclopentyl-N-cyclobutylformamide, isozyme beta(1)beta(1) in complex
	with inhibitors N-benzylformamide and N-heptylformamide, and isozyme
	gamma(2)gamma(2) in complex with inhibitor N-1-methylheptylformamide,
	X-ray diffraction structure determination and analysis at 1.45-2.5 A
	resolution, structure modeling) <109>
CR	#10# (isozyme YADH-1, crystal structure analysis) <120>
CR	#10# (trigonal crystal form alcohol dehydrogenase I: evidence for the
	existence of Zn ions in the crystal, from 20% PEG 4000, 20% 2-propanol,
	0.1 M sodium citrate, pH 5.6, and 1 mM NAD+, X-ray diffraction
	structure determination and analysis at 3.0 A resolution) <104>
CR	#10# (three-dimensional model of the enzyme structure suggest that Ca2+
	can be displaced by replacing Met-168 by an Arg residue) <247>
CR	#13# (enzyme in complex with trifluoroethanol and without NAD+, X-ray
	diffraction structure determination and analysis at 2.35 A resolution)
	<112>
CR	#26# (ternary complex of enzyme with NADH and ethylene glycol, X-ray
	diffraction structure determination and analysis at 2.3 A resolution,
	molecular replacement method) <129>
CR	#40# <30,34,35>
CR	#40# (10 mg/ml purified double mutant H51Q/K228R in complex with NAD+
	and 2,3- or 2,4-difluorobenzyl alcohol, in 50 mM ammonium
	N-[tris(hydroxymethyl)-methyl]-2-aminoethanesulfonate, pH 7.0, 5°C, 1
	mM NAD+, 10 mM 2,3-difluorobenzyl alcohol or 2,4-difluorobenzyl
	alcohol, equilibrated against increasing concentrations of
	2-methyl-2,4-pentanediole, crystal formation at 12%
	2-methyl-2,4-pentanediole, X-ray diffraction structure determination
	and analysis) <111>
CR	#40# (1 A resolution crystal structures of liver alcohol dehydrogenase
	in complex with NADH and two inhibitors: dimethyl sulfoxide and
	isobutyramide) <175>
CR	#45# (holo-enzyme form and apo-enzyme form) <56>
CR	#45# (apoenzyme and ternary complex of enzyme with NADH and
	2-ethoxyethanol bound to each subunit, X-ray diffraction structure
	determination and analysis at 2.3 A resolution) <108>
CR	#45# (microbatch method) <157>
CR	#45# (microbatch method in 100 mM Tris-HCl (pH 7.8), 10 mM
	dithiotreitol with the same volume of 12% (w/v) PEG 4000, 12% (v/v)
	2-propanol, 100 mM sodium citrate (pH 5.6) at 20°C) <161>
CR	#45# (twinned crystals are grown with the sitting drop vapour diffusion
	method using 2-methyl-2,4-pentanediol (50% v/v), Tris/HCl buffer (150
	mM, pH 8.4), and NADH (1 mM), prismatic crystals are grown at 4°C and
	20°C by microbatch and free interface diffusion methods with Tris/HCl
	buffer (130 mM, pH 8.0), NADH (2 mM), polyethyleneglycol 4000 (16%
	w/v), propan-2-ol or propan-1-ol (16% v/v) in trisodium citrate (100
	mM, pH 4.8-5.6)) <152>
CR	#47# (purified recombinant N-terminally His-tagged Adh3, hanging drop
	vapour diffusion method, mixing of 0.002 ml of 80mg/ml protein in 50 mM
	Tris, pH 7.0, with 0.002 ml of reservoir solution, comprising 0.1 M
	MES, pH 6.5, 16% w/w PEG 20000, and 0.001 ml of 50 mM CaCl2, 20°C,
	X-ray diffraction structure determination and analysis) <223>
CR	#77# <38>
CR	#83# (enzyme-NADP+-cofactor complex, X-ray diffraction strcuture
	determination and analysis, computational structure modeling) <125>
CR	#86# (multiple anomalous dispersion techniques, X-ray diffraction
	structure determination and analysis at 1.62 A resolution) <127>
CR	#104# <207>
CR	#104# (crystals are grown in the Advanced Protein Crystallization
	Facility during the Life and Microgravity Sciences Spacelab mission on
	the US Space Shuttle. Large diffracting crystals are obtained by
	dialysis, whereas only poor-quality crystals are obtained by vapour
	diffusion. The quality of both the microgravity and ground-based
	crystals is analysed by X-ray diffraction. There is some improvement in
	terms of size and diffraction resolution limit for the microgravity
	crystals. The twinning observed in the Earthgrown crystals is also
	present for those grown in microgravity) <216>
CR	#123# (the crystal structure of the binary complex SaADH2–NADH,
	determined at 1.75 A resolution, reveals details of the active site
	providing hints on the structural basis of the enzyme
	enantioselectivity) <218>
CR	#131# (the zinc-containing enzyme has been crystallized by the
	sitting-drop vapour-diffusion method using PEG 600 as precipitant.
	Single orthorhombic crystals with maximum dimensions of 0.4 * 0.4 * 1
	mm grow from 0.1 M PIPES pH 6.75 containing 13% PEG 600 and 0.5 mM NADH
	in approximately four weeks. The crystals diffract to better than 1.5 A
	using synchrotron radiation and belong to the orthorhombic space group
	P2(1)2(1)2, with unit-cell parameters a = 100.7, b = 103.2, c = 67.5 A)
	<236>
CR	#143# (structural modeling of ethanol-tolerant mutant protein) <265>
CR	#148# (structure of the alcohol dehydrogenase domain of the ADHE
	protein 2.5 A resolution and docking of the aldehyde dehydrogenase
	domain. The aldehyde dehydrogenase and alcohol dehydrogenase domains of
	a single ADHE may form dimers with different ADHE monomers rather than
	both with the same molecule) <241>

PURIFICATION
PU	#1# <44>
PU	#2# <1>
PU	#4# <8,65>
PU	#4# (alleloenzymes Adhf and Adhus) <58>
PU	#4# (alleloenzyme Adh71k) <63>
PU	#5# (liver isoenzyme A2 and B2 and stomach isoenzyme C2) <48>
PU	#5# (recombinant isozymes from Escherichia coli strain BL21) <119>
PU	#6# <169>
PU	#8# <12,15>
PU	#8# (class I isoenzymes) <13>
PU	#8# (anodic enzyme form) <18>
PU	#8# (isoenzyme beta3,beta3) <20>
PU	#8# (class III isoenzyme chi-ADH) <16>
PU	#8# (class II isoenzyme: pi-ADH) <14>
PU	#8# (recombinant ADH2 alloenzymes from Escherichia coli by DEAE and AMP
	or blue Sepharose chromatography, and ultrafiltration) <115>
PU	#8# (recombinant enzyme from Escherichia coli by DEAE ion exchange,
	5'-AMP-resin affinity, and Mono Q ion exchange chromatography) <124>
PU	#8# (recombinant isozymes from Escherichia coli strain BL21) <119>
PU	#9# (ADH-1, ADH-2 and ADH-3) <49>
PU	#9# (isoenzyme 1, 2, 3, and 4) <51>
PU	#10# <3,87>
PU	#10# (mutant enzyme S109P/L116S/Y294) <193>
PU	#10# (DEAE-Sepharose CL-4B column chromatograhy and octyl-Sepharose
	column chromatography) <202>
PU	#10# (using reactive Green 19 covalently immobilized ontomagnetic
	poly(2-hydroxyethyl methacrylate) nanostructures. Maximum alcohol
	dehydrogenase adsorption capacity is 176.09 mg/g polymer. Alcohol
	dehydrogenase molecules are desorbed by using 1.0 M NaCl with 98.4%
	recovery, purification is 45.63fold in a single step) <270>
PU	#12# <45>
PU	#12# (class I isoenzyme) <46>
PU	#13# (reombinant fusion enzyme by glutathione affinity chromatography,
	cleavage of GST fusion tag by thrombin, further purification of the
	active enzyme) <126>
PU	#14# <81>
PU	#18# <75,76>
PU	#18# (wild-type enzyme Adh1-1S and mutant enzyme Adh1-1S1108) <97>
PU	#19# <71>
PU	#21# <72>
PU	#23# (partial by isopycnic sucrose gradient centrifugation) <128>
PU	#25# <188>
PU	#30# (recombinant enzyme) <181>
PU	#31# <73>
PU	#35# <47>
PU	#37# <85>
PU	#38# <3>
PU	#40# <26,42,92>
PU	#40# (SS-isoenzyme) <28>
PU	#41# <67,68>
PU	#42# <25>
PU	#43# <114>
PU	#43# (recombinant His-tagged enzyme by nickel affinity chromatography
	and gel filtration) <232>
PU	#44# <6>
PU	#45# <66,70,152,157,161>
PU	#45# (Blue A column chromatography) <153>
PU	#45# (DEAE-Sepharose Fast Flow column chromatography and G75 gel
	filtration) <154>
PU	#45# (DEAE-Sepharose Fast Flow column chromatography, Matrex Gel Red A
	column chromatography, and Blue A column chromatography) <163>
PU	#45# (HiLoad Superdex 200 gel filtration) <159>
PU	#45# (HiTrap heparin-Sepharose column chromatography, DEAE-Sepharose
	fast-flow column chromatography, and HiLoad Superdex S-75 gel
	filtration) <160>
PU	#45# (Toyopearl Butyl 650 S column chromatography, Q Sepharose fast
	flow column chromatography, Superose 12 prep-grade gel filtration, and
	TosoHaas G 2000 SWXL gel filtration) <165>
PU	#46# <149>
PU	#50# (ADHE cannot be solubilized from membrane with detergents such as
	1% Triton X-100 or 1% sulfobetaine 3-12. The enzyme is easily
	dissociated from membrane by high-salt buffers containing either 1.0 M
	NaCl or (NH4)2SO4 without detergents) <279>
PU	#51# (ADH-MII) <82>
PU	#53# <151>
PU	#54# <99>
PU	#56# <147>
PU	#57# <147>
PU	#58# <5>
PU	#60# (2 isozymes from cytosol by DEAE ion exchange, hydroxyl apatite,
	and gel filtration chromatography, ADH I 35fold, ADH II 21fold) <113>
PU	#66# <78>
PU	#67# (partial) <69>
PU	#68# (ADH-2 and ADH-3) <60>
PU	#69# <84>
PU	#71# <8>
PU	#74# <8,63>
PU	#75# <8>
PU	#76# <8>
PU	#77# <8>
PU	#78# <24>
PU	#80# (3 isoenzymes) <77>
PU	#81# (partial) <83>
PU	#82# <101>
PU	#84# (recombinant enzyme 1.5fold from Escherichia coli strain BL21
	(DE3)) <226>
PU	#87# (128fold to homogeneity by adenosine 5'-monophosphate affinity and
	Mono-Q ion exchange chromatography) <118>
PU	#91# <144>
PU	#92# <137>
PU	#93# (HIS-Select High Flow cartridge chromatography) <162>
PU	#94# (HiLoad Superdex 200 gel filtration) <159>
PU	#96# <168>
PU	#98# <173>
PU	#99# <171>
PU	#100# <185>
PU	#104# <207,220,221>
PU	#106# (DEAE-Sepharose column chromatography) <195>
PU	#110# (Sephacryl S-100 gel filtration) <213>
PU	#111# (ultracentrifugation and Sepabeads EB-QA405 chromatography) <197>
PU	#112# (DEAE-Sepharose CL-4B column chromatograhy and octyl-Sepharose
	column chromatography) <202>
PU	#118# <256>
PU	#121# <217>
PU	#122# <219>
PU	#123# <218>
PU	#125# (soluble recombinant His6-tagged BmADH protein from Escherichia
	coli strain BL21 (DE3) by nickel affinity chromatography) <231>
PU	#126# (recombinant His6-tagged enzyme from Echerichia coli strain BL21
	(DE3) by nickel affinity chromatography) <222>
PU	#127# (native (R)-specific alcohol dehydrogenase 37fold from strain
	IFO10003, by ammonium sulfate fractionation, and anion exchange and
	hydrophobic interaction chromatography to homogeneity) <225>
PU	#130# (native enzyme from liver by anion exchange and AMP affinity
	chromatography, and a second different step of anion exchange
	chromatography) <227>
PU	#131# <239>
PU	#132# (purified in one step by immobilized metal-affinity
	chromatography) <237>
PU	#148# <241>
PU	#150# <244>
PU	#260# (Talon Co2+-affinity column chromatography) <211>

RENATURED
REN	#10# (Zn2+ withdrawal by inactivation with Chelex 100, reactivation of
	the apoenzyme by addition of CuSO4, 1 h at 25°C, pH 7.6) <122>

GENERAL_STABILITY
GS	#10# (even at 50°C the stabilization effect of lipid membranes on the
	tertiary and quaternary structures of the liposomal YADH allows the
	enzyme to form its thermostable complex with NAD+ in liposomes) <179>
GS	#10# (enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via
	glutaraldehyde shows enhanced thermal stability and good durability in
	the repeated use after recovered by magnetic separations. Within 7
	cycles of usage, the remaining activity is about 100%, 89.15%, 79.42%,
	69.50%, 62.80%, 56.48%, and 48.26% of the first use) <182>
GS	#10# (the recycling stability of YADH in silica-coated alginate gel
	beads is found to be increased significantly mainly due to the
	effective inhibition of enzyme leakage by compact silica film) <184>
GS	#10# (sucrose, glucose, and betaine stabilize ADH substantially while
	D-ribose and sarcosine destabilize the enzyme) <203>
GS	#10# (ADH immobilized on derived attapulgite nanofibers via
	glutaraldehyde covalent binding retains higher activity over wider
	ranges of pH and temperature than those of the free enzyme. After
	shaking at 125 rpm at 35°C for 32 h, a rapid loss in activity is
	observed, and almost complete activity of immobilized enzyme is lost in
	52 h. The activity of immobilized ADH decreases to 80% of its initial
	value after four cycles of operation and afterwards gradually decreases
	with every reuse, but it retains 42% activity after eight cycles for
	bioreduction of ethyl 3-oxobutyrate.) <196>
GS	#10# (effects of salts on the rate constants of inactivation by heat of
	alcohol dehydrogenase YADH at 60.0°C. At high concentrations, some
	salts have stabilizing effects, while others are destabilizing. The
	effects of salts in the high concentration range examined can be
	described as follows: (decreased thermal stability) NaClO4, NaI =
	(C2H5)4NBr, NH4Br, NaBr = KBr = CsBr = (no addition), (CH3)4NBr, KCl,
	KF, Na2SO4 (increased thermal stability). The decreasing effect of
	NaClO4 controlls the thermal stability of the enzyme absolutely and is
	not compensated by the addition of Na2SO4, which stabilizes the enzyme)
	<148>
GS	#111# (the presence of a second phase of a water-insoluble solvent like
	hexane or octane has only minor effects on the enzyme, which retains
	80% of its activity, allowing the use of these solvents in
	aqueous/organic mixtures to increase the availability of low-water
	soluble substrates) <197>
GS	#12# (dialysis against 50 mM Tris-HCl buffer, stable after 5 h, 3% loss
	of activity after 1 day, 82% loss of activity after 6 days) <45>
GS	#12# (dithiothreitol stabilizes activity at all stages of purification)
	<46>
GS	#13# (highly stable against 0.1 M urea and 0.05% SDS) <126>
GS	#40# (the catalytic zinc ions have an important stabilizing effect on
	the tertiary and quaternary structure of the immobilized enzyme) <36>
GS	#41# (enzyme form ADH I is more stable during purification than enzyme
	form ADH-II) <67>
GS	#45# (does not require the presence of reducing agents to mantain its
	stability even at high temperature, evidently due to the lack in free
	cysteines) <163>
GS	#60# (isozymes are stabilized by MgCl2 and DTT during purification)
	<113>
GS	#8# (100fold purified enzyme is destroyed by freezing) <12>

ORGANIC_SOLVENT_STABILITY
OSS	#10,70# Pyridine (#10# inactivation <121>; #70# active, from 25°C up
	to 90°C, 3 h <121>) <121>
OSS	#10,70# toluene (#10# active, from 25°C up to 75°C, 3 h,
	stabilization of the enzyme at elevated temperature <121>; #70# active,
	from 25°C up to 90°C, 3 h <121>) <121>
OSS	#10,70# dimethylformamide (#70# 50% v/v, 20% remaining activity at 4°C
	or 25°C after 1-100 min <121>; #10# 50% v/v, 75% remaining activity at
	4°C after 100 min, 15% remaining activity after 100 min at 25°C
	<121>) <121>
OSS	#10,70# dodecane (#10# active, from 25°C up to 75°C, 3 h,
	stabilization of the enzyme at elevated temperature <121>; #70# active,
	from 25°C up to 90°C, 3 h <121>) <121>
OSS	#10,70,123# dioxane (#10# 50% v/v, 50% remaining activity at 4°C after
	100 min, 10% remaining activity after 100 min at 25°C <121>; #70# 50%
	v/v, about 95% remaining activity at 4°C or 25°C after 1-100 min
	<121>; #123# 17%, 160% of initial activity <219>) <121,219>
OSS	#10,70,149# octane (#10# active, from 25°C up to 75°C, 3 h,
	stabilization of the enzyme at elevated temperature <121>; #70# active,
	from 25°C up to 90°C, 3 h <121>; #149# 50%, about 90% of initial
	activity <243>) <121,243>
OSS	#118# Methanol (#118# 10%, 100% residual activity <256>) <256>
OSS	#118# Ethanol (#118# 10%, 86% residual activity <256>) <256>
OSS	#118# urea (#118# 0.1 M, 40% residual activity <256>) <256>
OSS	#118# 1-propanol (#118# 10%, 38% residual activity <256>) <256>
OSS	#118# 1-butanol (#118# 10%, 29% residual activity <256>) <256>
OSS	#122# acetonitrile (#122# 120–125% activation after incubation for 25
	h in the presence of 17% acetonitrile. High concentration (30%) result
	in enzyme inactivation to 5–30% of the initial values following 5 h
	incubation at 50°C <219>) <219>
OSS	#122# 1,4-dioxane (#122# 30%, 5–30% inactivation of the initial
	values following 5 h incubation at 50°C <219>; #122# significant
	increases in enzyme activity occurs after 25 h incubation at a
	concentration of 30% <219>) <219>
OSS	#122# n-hexane (#122# significant increases in enzyme activity occurs
	after 25 h incubation at a concentration of 30% <219>) <219>
OSS	#122# methyl-tert-butylether (#122# significant increases in enzyme
	activity occurs after 25 h incubation at a concentration of 30% <219>)
	<219>
OSS	#122,123# Ethyl acetate (#122# significant increases in enzyme activity
	occurs after 25 h incubation at a concentration of 30% <219>; #123#
	30%, 180% of initial activity <219>) <219>
OSS	#122,123# n-heptane (#122# significant increases in enzyme activity
	occurs after 25 h incubation at a concentration of 30% <219>; #123#
	30%, 180% of initial activity <219>) <219>
OSS	#123# tert-butylmethyl ether (#123# 30%, 210% of initial activity
	<219>) <219>
OSS	#149# hexane (#149# 50%, about 95% of initial activity <243>) <243>
OSS	#153# propan-2-ol (#153# 10% v/v, enzyme catalyzes reduction of
	fluorinated ketones without addition of NADH <280>) <280>
OSS	#43# Acetone (#43# 50% v/v, stable at <114>) <114>
OSS	#43,122,149# 2-propanol (#43# 80% v/v, stable at <114>; #122#
	120–125% activation after incubation for 25 h in the presence of 17%
	2-propanol. High concentration (30%) result in enzyme inactivation to
	5–30% of the initial values following 5 h incubation at 50°C <219>;
	#149# 20%, about 110% of initial activity <243>) <114,219,243>
OSS	#43,47,149# more (#43# chemotolerant enzyme <114>; #47# Adh3 exhibits
	tolerance to several organic solvents <223>; #149# enzyme shows high
	resistance to organic solvents <243>) <114,223,243>
OSS	#55# isopropanol (#55# 20% v/v, 70% residual activity <255>) <255>
OSS	#55,105,108,150# DMSO (#105,108# DMSO is not an ideal
	substrate-delivering solvent for ADH-catalysed reactions <214>; #150#
	20% v/v, 24 h, 87% residual activity <244>; #55# 20% v/v, 70% residual
	activity <255>) <214,244,255>

OXIDATION_STABILITY
OS	#10# (among all the cysteine residues, Cys43 is the most susceptible to
	H2O2 oxidation, and the major oxidation products of this cysteine are
	Cys-SO2H and Cys-SO3H. The oxidation of Cys43 might be responsible for
	the inactivation of the enzyme upon H2O2 treatment) <189>
OS	#10# (Adh1p is oxidatively modified during ageing and, consequently,
	its activity becomes reduced) <190>
OS	#54# (pronounced oxygen lability at pH 9, even at pH 7, 2 h under air,
	80% loss of activity) <99>

PH_STABILITY
PHS	#10# 6-8 (#10# at pH 6.0 and 8.0, the activity of free ADH decreases
	dramatically during the incubation, and 90 min later most of the
	activity is lost, the immobilized form retains 81% of activity at pH
	8.0 <196>) <196>
PHS	#10# 6.5-9 (#10# native Zn-ADH enzyme <122>) <122>
PHS	#10# 6.5 (#10# below, Cu-ADH and Co-ADH <122>) <122>
PHS	#121# 4-10 (#121# 30 min, 50°C, no loss of activity <217>) <217>
PHS	#121# 3.3 (#121# 30 min, 50°C, 50% loss of activity <217>) <217>
PHS	#125# 8-9 (#125# purified recombinant His-tagged enzyme, 10 min, high
	stability within this range <231>) <231>
PHS	#18# 6-9 (#18# isoenzyme 2 and isoenzyme 3 <75>) <75>
PHS	#20# 11 (#20# rapid loss of activity <284>) <284>
PHS	#27# 6.5-7 (#27# most stable at <74>) <74>
PHS	#30# 4 (#30# 30°C, 1 h, 30% loss of activity <181>) <181>
PHS	#30# 5 (#30# 30°C, 1 h, 20% loss of activity <181>) <181>
PHS	#30# 6-11 (#30# 30°C, 1 h, less than 10% loss of activity <181>) <181>
PHS	#30,121# 1-2 (#30# 30°C, 1 h, 15% loss of activity <181>; #121# 30
	min, 50°C, 50% loss of activity <217>) <181,217>
PHS	#41# 7.5 (#41# 4°C, stable for 2 days <68>) <68>
PHS	#43# 5.5-6.3 (#43# purified recombinant enzyme expressed from Hansenula
	polymorpha, at least 80% of the initial activity is retained after 4
	min, 30°C <232>) <232>
PHS	#43# 5.8-6.6 (#43# purified recombinant enzyme expressed from Arxula
	adeninivorans, at least 80% of the initial activity is retained after 4
	min, 30°C <232>) <232>
PHS	#43# 5.2-6.3 (#43# purified recombinant enzyme expressed from
	Saccharomyces cerevisiae, at least 80% of the initial activity is
	retained after 4 min, 30°C <232>) <232>
PHS	#8# 7-10.6 (#8# stable <12>) <12>
PHS	#92# 5-9.5 (#92# 25°C, 1 h, stable <137>) <137>
PHS	#96# 4-8 (#96# 4°C, 48 h, stable <168>) <168>

STORAGE_STABILITY
SS	#111# (-20°C, several months, no loss of activity) <197>
SS	#118# (15°C, 50 mM sodium phosphate buffer, pH 8.0, half-life of
	wild-type 7 h, half-life of mutant C257L 17 h) <246>
SS	#118# (4°C, 50 mM sodium phosphate buffer, pH 7.0, 10 mM
	2-mercaptoethanol, 10% glycerol, both wild-type and mutant C357L stable
	for several months) <246>
SS	#12# (4°C, in presence of 1.0 mM dithiothreitol, stable for 10 days)
	<45>
SS	#132# (-20°C, inactive after approximately 2 weeks, storage at -80°C
	or lyophilization does not improve storage time) <237>
SS	#18# (-20°C, isoenzyme 2 is stable in 50% ethylene glycol for at least
	3 months, isoenzyme 1 and 3 maintain less than 50% of their original
	activity after 2 weeks) <75>
SS	#41# (4°C, most stable at pH 7.5 during storage for 2 days) <68>
SS	#43# (very stable during storage) <114>
SS	#45# (-20°C, 1 M NaCl in 20 mM Tris-HCl (pH 8.4) in the presence of an
	equal volume of glycerol, 12 months, no loss of activity) <163>
SS	#45# (4°C, 1 M NaCl in 20 mM Tris-HCl (pH 8.4) in the absence of
	glycerol, 4 months, 60% loss of activity) <163>
SS	#8# (4°C, pH 7.5, stable for 2-3 weeks) <14>
SS	#8# (4°C, 10 mM HEPES buffer, 1 mM dithioerythritol, pH 7.5, stable
	for 2 weeks) <16>
SS	#8# (4°C, 5 mM Na phosphate, pH 7.5, the half-life is 24 h. 0.01 mM
	ethanol effectively stabilizes for several weeks) <18>
SS	#8# (4°C, 5 mM Na-phosphate, pH 7.5, 50% loss of activity after 1 day.
	Enzyme can be stabilized for up to 2 weeks by storage in buffer
	containing 10 mM ethanol) <23>
SS	#91# (-20°C, 10 mM potassium phosphate buffer, pH 7.0, containing 0.5
	mM NAD+ without loss of activity for several months) <144>

TEMPERATURE_STABILITY
TS	#10# 56 (#10# native Zn-ADH enzyme <122>; #10# thermal aggregation
	occurs at 56°C, the thermal denaturation of ADH is irreversible <199>)
	<122,199>
TS	#10# 50-60 (#10# thermal unfolding of ADH is not observed below 60°C
	while the kinetic deactivation is observed even at 50°C <203>) <203>
TS	#10# 30-55 (#10# the specific activity of ADH decreases rapidly above
	30°C, ADH is almost completely inactive after a 36 min incubation at
	55°C <205>) <205>
TS	#10# 35-60 (#10# 58% of the original activity is retained after
	incubation of the immobilized enzyme at 35°C for 32 h, free enzyme
	loses 68% activity over a 60 min incubation at 60°C, whereas
	immobilized ADH retains 44% over a 60 min incubation at 60°C <196>)
	<196>
TS	#10# 69 (#10# Cu-ADH enzyme <122>) <122>
TS	#10,125,127# 25 (#127# purified native enzyme, stable up to <225>;
	#125# purified recombinant His-tagged enzyme, 10 min, completely stable
	up to <231>; #10# 6 h, more than 90% residual activity <285>)
	<225,231,285>
TS	#10,18,25,30,43,45,46,91,92,96,98,123# 50 (#46# 30 min, 50% loss of
	activity <149>; #45# 24 h, 30% loss of activity <66>; #30# 1 h, 15%
	loss of activity <181>; #18# wild-type enzyme Adh1-1S is more stable
	than mutant enzyme Adh1-1S1108 <97>; #96# 60 min, about 50% loss of
	activity <168>; #43# half-life: 35 h <114>; #10# stable up to, about
	20% remaining activity after 3 h <121>; #92# 1 h in 20 mM Tris-HCl
	buffer, pH 7.0, retains 70% of its activity <137>; #91# half-life: 304
	min in absence of NAD+ <144>; #25# 1 h, 90 mM potassium phosphate
	buffer, pH 6.5, complete loss of activity <188>; #98# half-life: 96 min
	<173>; #123# 24 h, 109% of initial activity <219>)
	<66,97,114,121,137,144,149,168,173,181,188,219>
TS	#10,25,40# 45 (#25# 1 h, 90 mM potassium phosphate buffer, pH 6.5, 70%
	loss of activity <188>; #10# 2 h, free YADH is increasingly deactivated
	during its incubation with decrease of the enzyme concentration from
	3.3 to 0.01 mg/ml because of the dissociation of tetrameric YADH into
	its subunits <179>; #40# thermal denaturation starts above 45°C. The
	conformational lock number is 2 when calculated both experimentally and
	computationally. The enzyme becomes monomer at 46°C, its activity
	starts to decrease at this temperature. The activity decreases to only
	11% of the native ADH activity with a two-phase manner at 49°C. The
	subunits are dissociated and several intermediates appear <277>; #10#
	complete loss of activity within 6 h <285>) <179,188,277,285>
TS	#10,27,30,45,91,92,96,98,113,114# 60 (#96# 60 min, complete loss of
	activity <168>; #45# half-life: 20 h <66>; #27# denaturation above
	<74>; #30# 1 h, 20% loss of activity <181>; #92# 1 h in 20 mM Tris-HCl
	buffer, pH 7.0, retains 24% of its activity <137>; #10# half-life: 2
	min in absence of NAD+ <144>; #91# half-life: 50 min in absence of
	NAD+, 143 min in presence of 0.01 mM NAD+ <144>; #98# half-life: 55 min
	<173>; #10# 60 min, about 35% loss of activity, soluble enzyme and
	enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via
	glutaraldehyde <182>; #113,114# 14 h, more than 50% of initial activity
	<215>) <66,74,137,144,168,173,181,182,215>
TS	#10,30,43,45,87,91,92,98,121,122,123,131# 70 (#131# 30 min, no loss of
	activity <239>; #98# half-life: 42 min <173>; #45# half-life: 5 h <66>;
	#30# 1 h, 40% loss of activity <181>; #10# above, Co-ADH enzyme <122>;
	#87# stable upt to <118>; #92# 1 h in 20 mM Tris-HCl buffer, pH 7.0,
	complete loss of activity <137>; #91# half-life: 6 min in absence of
	NAD+ <144>; #45# remains quite stable at 70°C in the absence of
	chelating agents <163>; #121# 10 min, stable. 120 min, 50% loss of
	activity <217>; #122# pH 9.0, 50 mM Tris-HCl, 24% loss of acrtivity
	<219>; #43# purified recombinant enzyme expressed from Hansenula
	polymorpha, over 80% of the initial activity is retained after 60 min
	<232>; #123# 24 h, 76% of initial activity <219>)
	<66,118,122,137,144,163,173,181,217,219,232,239>
TS	#10,41,45,91# 65 (#41# inactivation constant for ADHI: 1.23 per min,
	inactivation constant for ADH II: 0.13 per min <68>; #45# pH 8.0,
	protein concentration 2.5 mg/ml, 16 h, stable. 50% loss of activity
	after 8 h at protein concentration of 0.5 mg/ml <70>; #91# half-life:
	20 min in absence of NAD+ <144>; #45# at 65°C the half-lives of the
	native and carboxymethylated enzymes are 9 h and 4 h, respectively
	<153>; #45# the activity of the recombinant wild type enzyme slowly
	decreases to 50% after 16 h at 65°C <165>; #10# 60 min, about 80% loss
	of activity of soluble enzyme, about 55% loss of activity of enzyme
	covalently immobilized to magnetic Fe3O4 nanoparticles via
	glutaraldehyde <182>) <68,70,144,153,165,182>
TS	#10,87,123# 75 (#123# 30 min, stable up to <218>; #10# inactivation
	<121>; #87# and above, rapid loss of activity <118>) <118,121,218>
TS	#104# 65-88 (#104# the single and double mutant are less
	thermoresistant than the wild type enzyme, displaying a transition
	temperature of 78 and 88°C, respectively, which are 17 and 7°C lower
	than that of the wild-type enzyme. At 65°C the single mutant W95L is
	10fold less active and the double mutant W95L/N249Y is about 6fold more
	active than wild type enzyme, the reaction rate catalyzed by the double
	mutant W95L/N249Y increases more markedly than that of the wild type
	enzyme up to a temperature of about 83°C and then decreases rapidly
	due to thermal inactivation. The reaction rate of the single mutant
	W95L increases more slowly up to about 80°C and then decreases
	rapidly. At 65°C the single mutant is 10fold less active and the
	double mutant is about 6fold more active than wild type enzyme. <207>)
	<207>
TS	#118# 62.6 (#118# wild-type, thermal denaturation midpoint <246>) <246>
TS	#118# 65.3 (#118# mutant C257L, thermal denaturation midpoint <246>)
	<246>
TS	#123# 88 (#123# 30-min half-inactivation temperature <218>) <218>
TS	#13# 68 (#13# purified recombinant enzyme, most stable at <126>) <126>
TS	#13,45,87# 85 (#45# pH 8.0, protein concentration 0.5 mg/ml, 3 h, 50%
	loss of activity <70>; #13# remaining activity <126>; #87# slight
	residual activity <118>) <70,118,126>
TS	#131# 98 (#131# the enzyme maintains 24% of the original catalytic
	activity after incubation for 30 min <239>) <239>
TS	#142# 100 (#142# half-life 130 min <138>) <138>
TS	#18,40,45,70,150# 55 (#18# 60 min, 73% loss of activity of enzyme 1,
	10% loss of activity of enzyme 2, 21% loss of activity of enzyme 3
	<75>; #45# the native enzyme remains completely stable after heating
	for 3 h at 55°C while the carboxymethylated enzyme loses 10% of
	activity under the same conditions <153>; #70# ADH is insensitive to
	thermal stress at 55°C and remains fully active after a 36 min
	incubation at 55°C <205>; #40# ADH loses less than 30% of its initial
	activity after a 36 min incubation at 55°C <205>; #150# half-life 6.2
	h <244>) <75,153,205,244>
TS	#25,92,98# 30 (#98# half-life: 114 min <173>; #92# 1 h in 20 mM
	Tris-HCl buffer, pH 7.0, stable below <137>; #25# 1 h, 90 mM potassium
	phosphate buffer, pH 6.5, stable <188>) <137,173,188>
TS	#30,37,44,50,92,96,98,127# 40 (#37# stable below <85>; #30# 1 h, stable
	<181>; #96# 60 min, stable up to <168>; #98# half-life: 110 min <173>;
	#50# inactivation above <279>; #44# 60 min, stable <6>; #92# 1 h in 20
	mM Tris-HCl buffer, pH 7.0, retains 80% of its activity <137>; #127#
	purified enzyme, inactivation <225>) <6,85,137,168,173,181,225,279>
TS	#30,55,98,131,139# 80 (#139# stable up to <254>; #30# 1 h, 50% loss of
	activity <181>; #98# half-life: 18 min <173>; #131# 30 min, about 20%
	loss of activity <239>; #55# 5 h, more than 60% residual activity
	<255>) <173,181,239,254,255>
TS	#37# -20 (#37# loss of activity after 24 h <85>) <85>
TS	#40,46# 35 (#46# 30 min, no significant loss of activity <149>; #40#
	HLAD is a mesophilic enzyme whose activity and stability are
	significantly impaired at temperatures over 35°C <204>) <149,204>
TS	#43# 38.5-42.5 (#43# purified recombinant enzyme expressed from Arxula
	adeninivorans, at least 80% of the initial activity is retained after 4
	min <232>; #43# more than 80% of maximum activity, recombinant enzyme
	expressed in Arxula adeninivorans <232>) <232>
TS	#43# 32-41 (#43# purified recombinant enzyme expressed from
	Saccharomyces cerevisiae, at least 80% of the initial activity is
	retained after 4 min <232>; #43# more than 80% of maximum activity,
	recombinant enzyme expressed in Saccharomyces cerevisiae <232>) <232>
TS	#43# 34-38 (#43# purified recombinant enzyme expressed from Hansenula
	polymorpha, at least 80% of the initial activity is retained after 4
	min <232>; #43# more than 80% of maximum activity, recombinant enzyme
	expressed in Hansenula polymorpha <232>) <232>
TS	#45# 70-80 (#45# wild type and mutant enzyme N249Y are stable at 70°C,
	the mutant enzyme seems more thermoresistant than the wild type enzyme
	up to a temperature of 80°C, after which its activity decreases
	abruptly <154>) <154>
TS	#45,93,149# 95 (#93# activity increases with temperature up to 95°C
	<162>; #45# stable and active up to 95°C <152>; #149# half-life 4.5 h
	<243>) <152,162,243>
TS	#45,94# 85-90 (#94# half-life of 3 h at 85°C and 1 h at 90°C <159>;
	#45# half-life of 3 h at 85°C and 1 h at 90°C, the catalytic
	efficiency is considerably higher at temperatures below 90°C <159>)
	<159>
TS	#6# 73 (#6# inactivation above <169>) <169>
TS	#6,30,45,70,98,122,123# 90 (#70# stable up to <121>; #98# half-life: 4
	min <173>; #6,123# half-life 30 min <169,219>; #45# at 90°C the
	specific activity is about three times as high as that measured at
	65°C <163>; #30# 1 h, 95% loss of activity <181>; #122#
	half-inactivation temperature is 30 min <219>) <121,163,169,173,181,219>
TS	#8# 23 (#8# unstable at room temperature and above <12>) <12>
TS	#8,10,13,40,43# -999 (#40# distinct subunits have different
	deactivation properties <37>; #10# effect of salts in the high
	concentration range on the thermal stability <148>; #40#
	alpha-cyclodextrin causes thermal stabilization and delays the onset of
	secondary structural unfolding and aggregation by approx. 10°C and the
	midpoint temperatures by more than 5°C. alpha-Cyclodextrin diminishes
	the deactivation of the enzyme, decreasing the deactivation constant by
	more than 50%, and clearly reveals the stabilization of the enzyme not
	only structurally but also kinetically at higher temperatures <178>;
	#43# temperature stability profiles of recombinantly expressed enzymes,
	overview <232>) <37,112,115,148,178,232>

REFERENCE
RF	<1> Talbot, B.G.; Qureshi, A.A.; Cohen, R.; Thirion, J.P.: Purification
	and properties of two distinct groups of ADH isozymes from Chinese
	hamster liver. Biochem. Genet. (1981) 19, 813-829. {Pubmed:6794566}
RF	<2> Fong, W.P.: Isolation and characterization of grass carp
	(Ctenopharyngodon idellus) liver alcohol dehydrogenase. Comp. Biochem.
	Physiol. B (1991) 98, 297-302. {Pubmed:}
RF	<3> Pessione, E.; Pergola, L.; Cavaletto, M.; Giunta, C.; Trotta, A.;
	Vanni, A.: Extraction, purification and characterization of ADH1 from
	the budding yeast Kluyveromyces marxianus. Ital. J. Biochem. (1990) 39,
	71-82. {Pubmed:2193901}
RF	<4> Leblova, S.; El Ahmad, M.: Characterization of alcohol
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RF	<267> Chung, D.; Cha, M.; Guss, A.M.; Westpheling, J.: Direct
	conversion of plant biomass to ethanol by engineered
	Caldicellulosiruptor bescii. Proc. Natl. Acad. Sci. USA (2014) 111,
	8931-8936. {Pubmed:24889625}
RF	<268> Campbell, E.; Chuang, S.; Banta, S.: Modular exchange of
	substrate-binding loops alters both substrate and cofactor specificity
	in a member of the aldo-keto reductase superfamily. Protein Eng. Des.
	Sel. (2013) 26, 181-186. {Pubmed:23175796}
RF	<269> Pennacchio, A.; Giordano, A.; Esposito, L.; Langella, E.; Rossi,
	M.; Raia, C.A.: Insight into the stereospecificity of short-chain
	thermus thermophilus alcohol dehydrogenase showing pro-S hydride
	transfer and prelog enantioselectivity. Protein Pept. Lett. (2010) 17,
	437-443. {Pubmed:19807673}
RF	<270> Kaya, N.; Aktas Uygun, D.; Akgoel, S.; Denizli, A.: Purification
	of alcohol dehydrogenase from Saccharomyces cerevisiae using magnetic
	dye-ligand affinity nanostructures. Appl. Biochem. Biotechnol. (2013)
	169, 2153-2164. {Pubmed:23408231}
RF	<271> Takeda, M.; Anamizu, S.; Motomatsu, S.; Chen, X.; Thapa Chhetri,
	R.: Identification and characterization of a mycobacterial
	NAD+-dependent alcohol dehydrogenase with superior reduction of
	diacetyl to (S)-acetoin. Biosci. Biotechnol. Biochem. (2014) 78,
	1879-1886. {Pubmed:25082080}
RF	<272> Hong, S.H.; Ngo, H.P.; Kang, L.W.; Oh, D.K.: Characterization of
	alcohol dehydrogenase from Kangiella koreensis and its application to
	production of all-trans-retinol. Biotechnol. Lett. (2015) 37, 849-856.
	{Pubmed:25481533}
RF	<273> Chi, Y.C.; Lee, S.L.; Lai, C.L.; Lee, Y.P.; Lee, S.P.; Chiang,
	C.P.; Yin, S.J.: Ethanol oxidation and the inhibition by drugs in human
	liver, stomach and small intestine: Quantitative assessment with
	numerical organ modeling of alcohol dehydrogenase isozymes. Chem. Biol.
	Interact. (2016) 258, 134-141. {Pubmed:27544634}
RF	<274> Spickermann, D.; Hausmann, S.; Degering, C.; Schwaneberg, U.;
	Leggewie, C.: Engineering of highly selective variants of Parvibaculum
	lavamentivorans alcohol dehydrogenase. ChemBioChem (2014) 15,
	2050-2052. {Pubmed:25169816}
RF	<275> Malver, O.; Sebastian, M.J.; Oppenheimer, N.J.: Alteration in
	substrate specificity of horse liver alcohol dehydrogenase by an
	acyclic nicotinamide analog of NAD(+). DNA Repair (2014) 23, 95-100.
	{Pubmed:25280628}
RF	<276> Kasprzak, J.; Rauter, M.; Riechen, J.; Worch, S.; Baronian, K.;
	Bode, R.; Schauer, F.; Kunze, G.: Characterization of an Arxula
	adeninivorans alcohol dehydrogenase involved in the metabolism of
	ethanol and 1-butanol. FEMS Yeast Res. (2016) 16, FEHLT.
	{Pubmed:26912215}
RF	<277> Moosavi-Movahedi, F.; Saboury, A.A.; Alijanvand, H.H.; Bohlooli,
	M.; Salami, M.; Moosavi-Movahedi, A.A.: Thermal inactivation and
	conformational lock studies on horse liver alcohol dehydrogenase:
	structural mechanism. Int. J. Biol. Macromol. (2013) 58, 66-72.
	{Pubmed:23548863}
RF	<278> Jadhav, S.B.; Bankar, S.B.; Granstroem, T.; Ojamo, H.; Singhal,
	R.S.; Survase, S.A.: Interaction of carbohydrates with alcohol
	dehydrogenase: Effect on enzyme activity. J. Biosci. Bioeng. (2015)
	120, 252-256. {Pubmed:25670482}
RF	<279> Tsuji, K.; Yoon, K.S.; Ogo, S.: Biochemical characterization of a
	bifunctional acetaldehyde-alcohol dehydrogenase purified from a
	facultative anaerobic bacterium Citrobacter sp. S-77. J. Biosci.
	Bioeng. (2016) 121, 253-258. {Pubmed:26216639}
RF	<280> Borzecka, W.; Lavandera, I.; Gotor, V.: Synthesis of enantiopure
	fluorohydrins using alcohol dehydrogenases at high substrate
	concentrations. J. Org. Chem. (2013) 78, 7312-7317. {Pubmed:23796348}
RF	<281> Keller, M.W.; Lipscomb, G.L.; Nguyen, D.M.; Crowley, A.T.; Schut,
	G.J.; Scott, I.; Kelly, R.M.; Adams, M.W.: Ethanol production by the
	hyperthermophilic archaeon Pyrococcus furiosus by expression of
	bacterial bifunctional alcohol dehydrogenases. Microb. Biotechnol.
	(2017) FEHLT, 0000. {Pubmed:28194879}
RF	<282> Laadan, B.; Wallace-Salinas, V.; Carlsson, A.J.; Almeida, J.R.;
	Radstroem, P.; Gorwa-Grauslund, M.F.: Furaldehyde substrate specificity
	and kinetics of Saccharomyces cerevisiae alcohol dehydrogenase 1
	variants. Microb. Cell Fact. (2014) 13, 112. {Pubmed:25287956}
RF	<283> Atteia, A.; van Lis, R.; Mendoza-Hernández, G.; Henze, K.;
	Martin, W.; Riveros-Rosas, H.; González-Halphen, D.: Bifunctional
	aldehyde/alcohol dehydrogenase (ADHE) in chlorophyte algal
	mitochondria. Plant Mol. Biol. (2003) 53, 175-188. {Pubmed:14756315}
RF	<284> Cheng, F.; Hu, T.; An, Y.; Huang, J.; Xu, Y.: Purification and
	enzymatic characterization of alcohol dehydrogenase from Arabidopsis
	thaliana. Protein Expr. Purif. (2013) 90, 74-77. {Pubmed:23707506}
RF	<285> Wang, H.; Xiao, D.; Zhou, C.; Wang, L.; Wu, L.; Lu, Y.; Xiang,
	Q.; Zhao, K.; Li, X.; Ma, M.: YLL056C from Saccharomyces cerevisiae
	encodes a novel protein with aldehyde reductase activity. Appl.
	Microbiol. Biotechnol. (2017) 101, 4507-4520. {Pubmed:28265724}

ACTIVATING_COMPOUND
AC	#10# Glutaraldehyde (#10# treating with 0.5% glutaraldehyde solution,
	the activity of the immobilized enzyme is at maximum <196>) <196>
AC	#111# Urea (#111# 130% relative activity at 1 M <197>) <197>
AC	#111# Triton X-100 (#111# 201% relative activity at 10% (v/v) <197>)
	<197>
AC	#122# 2-propanol (#122# 120–125% activation after incubation for 25 h
	in the presence of 17% 2-propanol. High concentration (30%) result in
	enzyme inactivation to 5–30% of the initial values following 5 h
	incubation at 50°C <219>) <219>
AC	#122# 1,4-dioxane (#122# significant increases in enzyme activity
	occurs after 25 h incubation at a concentration of 30% <219>) <219>
AC	#122# n-hexane (#122# significant increases in enzyme activity occurs
	after 25 h incubation at a concentration of 30% <219>) <219>
AC	#122# n-heptane (#122# significant increases in enzyme activity occurs
	after 25 h incubation at a concentration of 30% <219>) <219>
AC	#122# TBME (#122# significant increases in enzyme activity occurs after
	25 h incubation at a concentration of 30% <219>) <219>
AC	#123# 2-mercaptoethanol (#123# 5 mM, 112% of initial activity <219>)
	<219>
AC	#150# dithiothreitol (#150# 1 mM, 123% of initial activity <244>) <244>
AC	#25# iodoacetate (#25# 1 mM, 1.1fold activation <188>) <188>
AC	#40# Acetylsalicylate (#40# enhances activity <143>) <143>
AC	#40# tert-butyl hydroperoxide (#40# stimulation up to 100 mM <86>) <86>
AC	#40,128# more (#40# isonicotinimidylation and methylation increases
	activity <35>; #128# without heat treatment the AdhC enzyme shows no
	detectable activity, but after 10 min at higher temperatures the
	activity is revealed. The highest activity is measured after 10 min at
	100°C <230>) <35,230>
AC	#45# iodoacetamide (#45# 1 mM activates up to 25fold <163>) <163>
AC	#5# tert-butanol (#5# activates ADH3 <141>) <141>
AC	#5# butyramide (#5# activates ADH3 <141>) <141>
AC	#5# Valeramide (#5# activates ADH3 <141>) <141>
AC	#5# capronamide (#5# activates ADH3 <141>) <141>
AC	#5# S-nitrosoglutathione (#5# ADH3-mediated alcohol oxidation is
	promoted in the presence of S-nitrosoglutathione <200>) <200>
AC	#6,51,113,150# EDTA (#51# enhances activity <82>; #6# 10 mM, 1.65fold
	activation <169>; #150# 1 mM, 110% of initial activity <244>; #113# 1
	mM, 105% of initial activity <215>) <82,169,215,244>
AC	#86,122# acetonitrile (#122# 120–125% activation after incubation for
	25 h in the presence of 17% acetonitrile. High concentration (30%)
	result in enzyme inactivation to 5–30% of the initial values
	following 5 h incubation at 50°C <219>; #86# the enzyme is activated
	by water-miscible organic solvents <238>) <219,238>

KI_VALUE
KI	#10# 20.8 {5-hydroxymethylfurfural}  (#10# mutant S110P/Y295C, pH 6.7,
	30°C <282>) <282>
KI	#10# 0.025 {mithramycin}  (#10# in 50 mM Tris-HCl, pH 8.0 at 25°C
	<209>) <209>
KI	#10# 0.038 {mithramycin}  (#10# in 50 mM Tris-HCl, pH 8.0 at 25°C
	<209>) <209>
KI	#10# 46 {acetaldehyde}  (#10# mutant S110P/Y295C, pH 6.7, 30°C <282>)
	<282>
KI	#10# 1.32 {furfural}  (#10# mutant S110P/Y295C, pH 6.7, 30°C <282>)
	<282>
KI	#10# 12.53 {acetaldehyde}  (#10# wild-type, pH 6.7, 30°C <282>) <282>
KI	#10# 1363 {furfural}  (#10# wild-type, pH 6.7, 30°C <282>) <282>
KI	#105# 1.7 {ethanol}  (#105# isozyme ADH1C, using 1-hydroxymethylpyrene
	as substrate <214>) <214>
KI	#105# 1470 {ethanol}  (#105# isozyme ADH3, using 1-hydroxymethylpyrene
	as substrate <214>) <214>
KI	#108# 3.3 {ethanol}  (#108# isozyme ADH4, using 1-hydroxymethylpyrene
	as substrate <214>) <214>
KI	#118# 2.1 {Butyraldehyde}  (#118# wild-type, pH 8.0, 60°C <246>) <246>
KI	#26# 6.64 {4-Methylpyrazole}  <135>
KI	#33# 0.47 {4-Methylpyrazole}  <135>
KI	#40# 9.7 {Cyclohexanol}  (#40# pH 8.0, 25°C <275>) <275>
KI	#40# 96 {propan-2-ol}  (#40# pH 8.0, 25°C <275>) <275>
KI	#45# 0.13 {pyrazole}  (#45# apparent value <163>) <163>
KI	#45# 0.009 {4-Methylpyrazole}  (#45# apparent value <163>) <163>
KI	#45# 0.0032 {4-iodopyrazole}  (#45# apparent value <163>) <163>
KI	#5# 0.026 {Octanoic acid}  (#5# pH 7.5, 25°C, wild-type enzyme, versus
	NAD+ <110>) <110>
KI	#5# 0.072 {cyclohexylformamide}  (#5# pH 7.5, 25°C, wild-type enzyme,
	versus NADH <110>) <110>
KI	#5# 0.00008 {caffeic acid}  (#5# at 37°C in 0.1 M Na-K phosphate
	buffer (pH 7.4) <212>) <212>
KI	#5# 0.0051 {pyrazole}  (#5# at 37°C in 0.1 M Na-K phosphate buffer (pH
	7.4) <212>) <212>
KI	#5# 0.022 {ellagic acid}  (#5# at 37°C in 0.1 M Na-K phosphate buffer
	(pH 7.4) <212>) <212>
KI	#5# 0.035 {cyclohexylformamide}  (#5# pH 7.5, 25°C, wild-type enzyme,
	versus benzaldehyde <110>) <110>
KI	#5# 0.037 {Octanoic acid}  (#5# pH 7.5, 25°C, wild-type enzyme, versus
	octanol <110>) <110>
KI	#5# 0.0079 {Vanillin}  (#5# at 37°C in 0.1 M Na-K phosphate buffer (pH
	7.4) <212>) <212>
KI	#5# 0.0156 {syringaldehyde}  (#5# at 37°C in 0.1 M Na-K phosphate
	buffer (pH 7.4) <212>) <212>
KI	#65# 6.4 {4-Methylpyrazole}  <135>
KI	#7# 18.26 {4-Methylpyrazole}  <135>
KI	#8# 0.014 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	versus ethanol <116>) <116>
KI	#8# 0.028 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	versus NAD+ <116>) <116>
KI	#8# 0.0047 {5alpha-androstan-17beta-ol-3-one}  (#8# pH 7.3, 37°C,
	versus cyclohexanone <116>) <116>
KI	#8# 0.0047 {4-androsten-3,17-dione}  (#8# pH 7.3, 37°C, versus
	cyclohexanone <116>) <116>
KI	#8,23# -999 {more}  (#8# inhibition kinetics <116>) <116,123,124>

IC50_VALUE
IC50	#45# 1.7 {guanidine hydrochloride}  (#45# wild type enzyme <154>) <154>
IC50	#45# 2.2 {guanidine hydrochloride}  (#45# mutant enzyme N249Y <154>)
	<154>

PI_VALUE
PI	#102# 6.1 (#102# calculated <177>) <177>
PI	#103# 5.7 (#103# calculated <177>) <177>
PI	#110# 5.5 (#110# Ta1316 ADH, calculated from amino acid sequence <213>)
	<213>
PI	#118# 4.9 (#118# isoelectric focusing <256>) <256>
PI	#15# 8.3 (#15# calculated from sequence <172>) <172>
PI	#154# 4.8 (#154# isoelectric focusing <271>) <271>
PI	#154# 5.1 (#154# calculated <271>) <271>
PI	#157# 6.98 (#157# calculated from sequence <283>) <283>
PI	#47# 5.23 (#47# sequence calculation <223>) <223>
PI	#87# 6 <118>
PI	#97# 6.3 (#97# calculated from sequence, ADH1 <172>) <172>

IC50_VALUE
IC50	#45# 1.7 {guanidine hydrochloride}  (#45# wild type enzyme <154>) <154>
IC50	#45# 2.2 {guanidine hydrochloride}  (#45# mutant enzyme N249Y <154>)
	<154>

///
ID	6.3.5.8 (transferred to EC 2.6.1.85. As ATP is not hydrolysed during the reaction, the classification of the enzyme as a ligase was incorrect.)
********************************************************************************
*                                                                              *
* Copyrighted by Dietmar Schomburg, Techn. University Braunschweig, GERMANY    *
* Distributed under the License as stated at http:/www.brenda-enzymes.org      *
*                                                                              *
********************************************************************************

RECOMMENDED_NAME
RN	aminodeoxychorismate synthase


SYSTEMATIC_NAME
SN


///
ID	1.2.1.51
********************************************************************************
*                                                                              *
* Copyrighted by Dietmar Schomburg, Techn. University Braunschweig, GERMANY    *
* Distributed under the License as stated at http:/www.brenda-enzymes.org      *
*                                                                              *
********************************************************************************

PROTEIN
PR	#1# Euglena gracilis   <1,2,3,4,5,6,8,9>
PR	#2# Cryptosporidium parvum   <10>
PR	#3# Moniliella megachiliensis   <11>
PR	#4# Euglena gracilis Q94IN5  <7>

RECOMMENDED_NAME
RN	pyruvate dehydrogenase (NADP+)


SYSTEMATIC_NAME
SN	pyruvate:NADP+ 2-oxidoreductase (CoA-acetylating)


SYNONYMS
SY	#1,2# pyruvate:NADP+ oxidoreductase <9,10>
SY	#2# CpPNO <10>
SY	#3# PDH <11>
SY	#3# pyruvate dehydrogenase <11>

///
ID	2.7.11.2
********************************************************************************
*                                                                              *
* Copyrighted by Dietmar Schomburg, Techn. University Braunschweig, GERMANY    *
* Distributed under the License as stated at http:/www.brenda-enzymes.org      *
*                                                                              *
********************************************************************************

PROTEIN
PR	#1# Mammalia   <30,31,35>
PR	#2# Mus musculus   <23,37,39,45,56,75,77,81>
PR	#3# Homo sapiens
	<28,30,31,35,37,39,41,42,43,44,46,47,48,49,50,51,52,55,58,59,60,63,64
	65,66,67,68,71,77,81,82,92>
PR	#3# Mus musculus
	<28,30,31,35,37,39,41,42,43,44,46,47,48,49,50,51,52,55,58,59,60,63,64
	65,66,67,68,71,77,81,82,92>
PR	#4# Rattus norvegicus
	<5,18,21,23,27,29,30,31,32,33,34,35,37,39,42,48,53,57,60,69,76,79,80,81
	82>
PR	#5# Sus scrofa   <3,17>
PR	#6# Saccharomyces cerevisiae   <62>
PR	#7# Bos taurus   <1,2,3,6,7,8,9,10,11,12,13,14,15,20,30>
PR	#8# Oryctolagus cuniculus   <4>
PR	#9# Pisum sativum   <16>
PR	#10# Zea mays   <30>
PR	#11# Arabidopsis thaliana   <30,78>
PR	#12# Xenopus laevis   <40>
PR	#13# Caenorhabditis elegans   <25>
PR	#14# Homo sapiens Q16654 SwissProt <19,74,86,87,91>
PR	#14# Homo sapiens Q16654 UniProt <19,74,86,87,91>
PR	#15# Rattus norvegicus Q63065  <24,33,36>
PR	#15# Rattus norvegicus Q63065 SwissProt <24,33,36>
PR	#16# Ascaris suum O02623 SwissProt <22,25>
PR	#17# Arabidopsis thaliana Q9SBJ1  <26,38,54>
PR	#17# Arabidopsis thaliana Q9SBJ1 SwissProt <26,38,54>
PR	#18# Rhinolophus ferrumequinum Q1KMR4 SwissProt <61>
PR	#19# Sus scrofa C1IHT9 UniProt <73>
PR	#20# Rattus norvegicus Q64536  <72>
PR	#21# Homo sapiens Q15118  <70,84,87,89>
PR	#21# Homo sapiens Q15118 UniProt <70,84,87,89>
PR	#22# Xenopus tropicalis A9ULF7 UniProt <83>
PR	#23# Xenopus tropicalis Q6DFQ9 UniProt <83>
PR	#24# Brassica napus Q3LTL2 UniProt <85>
PR	#25# Homo sapiens Q15120 UniProt <87>
PR	#26# Mus musculus Q9JK42 UniProt <88>
PR	#27# Fusarium graminearum I1RE83 UniProt <90>
PR	#28# Mus musculus O70571 UniProt <88>
PR	#29# Homo sapiens Q15119 UniProt <87>

RECOMMENDED_NAME
RN	[pyruvate dehydrogenase (acetyl-transferring)] kinase


SYSTEMATIC_NAME
SN	ATP:[pyruvate dehydrogenase (acetyl-transferring)] phosphotransferase


SYNONYMS
SY	 kinase (phosphorylating), pyruvate dehydrogenase
SY	 pyruvate dehydrogenase kinase (phosphorylating)
SY	 pyruvate dehydrogenase kinase activator protein
SY	#1,3,4,12,15# More (#1,3,15# PDK isozymes and the related
	branched-chain dehydrogenase kinase form a unique family of serine
	kinases <30,36>; #4# enzyme possibly belongs to the ATPase/kinase
	family <24>; #12# enzyme belongs to the PDK family <40>) <24,30,36,40>
SY	#1,3,4,7,11,12,14,15,18,24# PDK
	<19,28,29,30,31,32,33,34,35,38,40,49,50,51,55,58,59,61,65,66,67,69,70
	78,85,92>
SY	#11# pyruvate dehydrogenase-kinase <78>
SY	#11# E1-kinase <78>
SY	#14# PDK 4 <86>
SY	#2# pyruvate dehydrogenase kinase isoenzyme 4 <56>
SY	#2# PDHK4 <56>
SY	#2,3,4,11,12,14,17,18,21,22,23,24,25,26,27,28,29# pyruvate
	dehydrogenase kinase
	<38,39,40,43,47,48,50,51,52,54,55,58,59,61,63,64,65,66,67,68,69,70,77
	83,85,87,88,89,90,92>
SY	#2,3,4,14,19# pyruvate dehydrogenase kinase 4
	<37,45,53,73,74,75,79,86,91>
SY	#2,3,4,14,19,23,28# PDK4 (#14,28# isoform <87,88>)
	<37,39,45,47,48,53,60,73,74,75,79,82,83,87,88,91>
SY	#2,3,4,21# pyruvate dehydrogenase kinase 1 <76,81,84>
SY	#2,3,4,21,27# PDK1 (#21# isoform <87>; #21# UniProt <84>)
	<37,47,48,55,81,84,87,90>
SY	#2,3,4,26,29# PDK2 (#26,29# isoform <87,88>)
	<37,43,47,48,52,60,71,77,87,88>
SY	#21# PDKH1 <84>
SY	#21# PDHK1 <89>
SY	#27# PKP1 <90>
SY	#3# pyruvate dehydrogenase kinase 3 <46>
SY	#3# PDK-2 <50>
SY	#3# PDK-4 <50>
SY	#3,4# PDH kinase <27,42,51>
SY	#3,4# pyruvate dehydrogenase kinase 2 <41,43,44,57,71,72,80>
SY	#3,4# PDHK2 <41,44,57,72,80>
SY	#3,4# pyruvate dehydrogenase kinase-4 <82>
SY	#3,4,17# PDHK <27,42,54,63,64,68>
SY	#3,4,22,25# PDK3 (#25# isoform <87>) <37,46,47,48,83,87>
SY	#4# PDH kinase 1 <76>

///
ID	2.4.99.20 ()
********************************************************************************
*                                                                              *
* Copyrighted by Dietmar Schomburg, Techn. University Braunschweig, GERMANY    *
* Distributed under the License as stated at http:/www.brenda-enzymes.org      *
*                                                                              *
********************************************************************************

PROTEIN
PR	#1# Mus musculus   <1>
PR	#2# Oryctolagus cuniculus   <4>
PR	#3# Homo sapiens P28907 UniProt <2,3,5,6,7>
PR	#4# Rattus norvegicus Q64244 SwissProt <1>
PR	#5# Aplysia californica P29241 UniProt <2,3,6>
PR	#6# Mus musculus P56528 UniProt <5,8>
PR	#7# Axinella polypoides   <3>

RECOMMENDED_NAME
RN	2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase


SYSTEMATIC_NAME
SN	NADP+:nicotinate ADP-ribosyltransferase


SYNONYMS
SY	#1,3,4,6# CD38 (#1,4# gene name <1>) <1,2,5>
SY	#1,4# diphosphopyridine nucleosidase (#1,4# ambiguous <1>) <1>
SY	#1,4# BST1 (#1,4# gene name <1>) <1>
SY	#3# ADPRC 1 <2>
SY	#3,5# 2'-phospho-cyclic-ADP-ribose transferase <2>
SY	#3,5# ADP-ribosyl cyclase 1 <2>

///
