Package: brendapy
brendapy: BRENDA in pythonThebrendapypackage provides a python parser and utility functions
for enzyme information fromBRENDA.
The parser extracts the all information split up by individual protein entries from the database flat file and makes it accessible in a simple manner.brendapysupport has been tested on pythonpy38,py39andpy310. Code is available fromhttps://github.com/matthiaskoenig/brendapy.This package was developed in the context of building kinetic pathway models with focus on extracting parameters likeKmorKifrom BRENDA.How to citeUse the following to citebrendapyin your project.If you use this package citeBRENDAChang A., Jeske L., Ulbrich S., Hofmann J., Koblitz J., Schomburg I., Neumann-Schaal M., Jahn D., Schomburg D.
BRENDA, the ELIXIR core data resource in 2021: new developments and updates. (2021), Nucleic Acids Res., 49:D498-D508.
DOI: 10.1093/nar/gkaa1025 PubMed: 33211880ContributingContributions are always welcome! Please read thecontributing guidelinesto
get started.LicenseSource Code:LGPLv3Documentation:CC BY-SA 4.0The brendapy source is released under both the GPL and LGPL licenses version 2 or
later. You may choose which license you choose to use the software under.This program is free software: you can redistribute it and/or modify it under
the terms of the GNU General Public License or the GNU Lesser General Public
License as published by the Free Software Foundation, either version 2 of the
License, or (at your option) any later version.This program is distributed in the hope that it will be useful, but WITHOUT ANY
WARRANTY; without even the implied warranty of MERCHANTABILITY or FITNESS FOR A
PARTICULAR PURPOSE. See the GNU General Public License for more details.FundingMatthias König was supported by the Federal Ministry of Education and Research (BMBF, Germany)
within the research network Systems Medicine of the Liver (LiSyM, grant number 031L0054)
and is supported by the German Research Foundation (DFG) within the Research Unit Programme FOR 5151
“QuaLiPerF(Quantifying Liver Perfusion-Function Relationship in Complex Resection -
A Systems Medicine Approach)” by grant number 436883643 and by grant number 465194077 (Priority Programme SPP 2311, Subproject SimLivA).Installationbrendapyis available frompypiand
can be installed via:pip install brendapyDevelop versionThe latest develop version can be installed via:pip install git+https://github.com/matthiaskoenig/brendapy.git@developOr via cloning the repository and installing via:git clone https://github.com/matthiaskoenig/brendapy.git
cd brendapy
pip install -e .To install for development use:pip install -e .[development]UsageExamples are provided in./src/brendapy/examples.pyand./tests/test_brendapy.py."""Example use case brendapy."""frombrendapyimportBrendaParserfrombrendapy.consoleimportconsoledefhuman_proteins_for_ec(ec:str="1.1.1.1")->None:"""Parse the human protein entries for a given EC number in BRENDA.

    Prints overview of number of proteins, protein ids, and human proteins.
    """brenda=BrendaParser()proteins=brenda.get_proteins(ec)console.print(f"{len(proteins)}proteins for EC{ec}in BRENDA")console.print(f"Protein identifier:{proteins.keys()}")console.print("-"*80)forpinproteins.values():ifp.organism=="Homo sapiens":console.print(p)console.rule()if__name__=="__main__":human_proteins_for_ec(ec="1.1.1.1")OrderedDict([('protein_id',107),('ec','1.1.1.1'),('organism','Homo sapiens'),('taxonomy',9606),('uniprot','P00326'),('CF',[{'comment':'#13,24,44,61,111,113,166# dependent on ''<113,114,126,128,197,210,292>; #122# specific for ''NAD+ <211>; #162# specific for <287>; #46,96# ''dependent <153,154,159>; #163# preferred cofactor ''<288>; #41# kinetics of coenzyme binding in the ''pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced ''conversion <62>; #41# NAD+ acts as an activator ''which induces an active form of the enzyme <34>; ''#41# preferred substrate <42>; #85# activity with ''mutants G223D/T224I and G223D/T224I/H225N <125>; ''#10# cofactor binding mode <120>; #120# dependent ''on, cofactor binding mechanism and conformation ''from crystal structure analysis <112>; #88# the ''monomer consists of a catalytic and a ''cofactor-binding domain, the cofactor is bound ''between 2 domains in a cleft <127>; ''#7,27,34,50,66# strongly preferred as cofactor ''<135>; #93# specific for NAD+, no activity with ''NADP+, pro-R stereospecificity for hydrogen ''transfer <144>; #99# ADH1 preferrs NAD+ 205fold ''better than NADP+ as cofactor <172>; #15# ADH3 ''does not react with NADP+ <172>; #144# 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>; #112# shows NAD+ as the preferred co-factor ''over NADP+ <213>; #41# 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>; #115# NAD+ is prefered over NADP+ <215>; ''#116# NADP+ is prefered over NAD+ <215>; #125# ''strict requirement for NAD(H) as the coenzyme, no ''activity with NADP+. The specificity constant ''value is 6fold higher for NADH than NAD+ <218>; ''#124# the enzyme transfers the deuteride to the ''Si-face of NAD+ <219>; #48# Adh3 is strictly ''dependent on NAD+/NADH, and shows no activity with ''NADP+/NADPH as cofactor <223>; #134# exclusively ''NAD+ dependent <237>; #51# 57fold preferred over ''NADP+ <279>; #23# H255R single mutant exhibits an ''increased binding affinity toward NADP+ and a ''concomitant reduction in affinity for NAD+ <290>; ''#23# insertion of an RTX domain from the adenylate ''cyclase of Bordetella pertussis into a loop near ''the catalytic active site of the thermostable ''alcohol dehydrogenase D from Pyrococcus furiosus. ''The resultant chimera, beta-AdhD, gains the ''calcium-binding ability of the beta-roll, retains ''the thermostable activity of AdhD, and exhibits ''reduced overall alcohol dehydrogenase activity. ''The addition of calcium to beta-AdhD ''preferentially inhibits NAD+-dependent activity in ''comparison to NADP+-dependent activity. Calcium is ''a competitive inhibitor of AdhD, and the addition ''of the RTX domain introduces calcium-dependent ''noncompetitive inhibition to beta-AdhD affecting ''NAD+-dependent activity <289>','data':'NAD+','refs':[1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74,75,76,77,78,79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98,99,100,101,102,103,105,110,111,112,113,114,115,116,118,120,121,124,125,126,127,128,129,130,135,136,137,138,139,141,143,144,146,148,149,152,153,154,156,157,158,159,161,162,163,164,165,169,172,180,194,195,196,197,198,200,201,202,203,204,205,206,207,208,209,210,211,212,213,214,215,217,218,219,220,221,222,223,225,226,227,229,230,231,232,233,234,237,243,252,254,256,257,260,269,272,279,286,287,288,289,290,292,293]}]),('ID','1.1.1.1'),('IN',[{'comment':'#100# 50% (v/v), 29% loss of activity <173>; #107# ''DMSO inhibits isozyme ADH2-catalysed oxidation in ''an uncompetitive mode and reduction in a mixed ''mode <214>; #107# DMSO inhibits isozymes ''ADH1C-catalysed oxidation in an uncompetitive mode ''and reduction in a mixed mode, no inhibition is ''detected with isozyme ADH3 <214>; #110# DMSO ''inhibits isozymes ADH4-catalysed oxidation in an ''uncompetitive mode and reduction in a mixed mode ''<214>','data':'DMSO','refs':[173,214]},{'comment':'#46# 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>; #36# isoenzyme AA-ADH, BB-ADH and ''TT-ADH <95>; #5# inhibits cell protein ''carbonylation following exposure to crotyl alcohol ''<117>','data':'4-Methylpyrazole','refs':[2,11,14,16,21,23,24,25,95,96,117,135,163,214]},{'comment':'#91# substrate inhibition above 0.5 M <105>; #100# ''50% (v/v), 59% loss of activity <173>; #107# ''ethanol competitively inhibits the oxidation of ''1-hydroxymethylpyrene by ADH1C and ADH3 <214>; ''#110# ethanol competitively inhibits the oxidation ''of 1-hydroxymethylpyrene by ADH4 <214>','data':'ethanol','refs':[105,173,214]}]),('KI',[{'chebi':'CHEBI:16236','comment':'#107# isozyme ADH1C, using 1-hydroxymethylpyrene ''as substrate <214>','data':'1.7 {ethanol}','refs':[214],'substrate':'ethanol','units':'mM','value':1.7},{'chebi':'CHEBI:16236','comment':'#107# isozyme ADH3, using 1-hydroxymethylpyrene as ''substrate <214>','data':'1470 {ethanol}','refs':[214],'substrate':'ethanol','units':'mM','value':1470.0}]),('KM',[{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.00024 {1-formyl-8-methylpyrene}','refs':[214],'substrate':'1-formyl-8-methylpyrene','units':'mM','value':0.00024},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.00031 {1-hydroxymethyl-8-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-8-methylpyrene','units':'mM','value':0.00031},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.00032 {1-formyl-6-methylpyrene}','refs':[214],'substrate':'1-formyl-6-methylpyrene','units':'mM','value':0.00032},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.00037 {4-hydroxymethylpyrene}','refs':[214],'substrate':'4-hydroxymethylpyrene','units':'mM','value':0.00037},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.00048 {2-hydroxymethylpyrene}','refs':[214],'substrate':'2-hydroxymethylpyrene','units':'mM','value':0.00048},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.0005 {1-formylpyrene}','refs':[214],'substrate':'1-formylpyrene','units':'mM','value':0.0005},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.00055 {1-formylpyrene}','refs':[214],'substrate':'1-formylpyrene','units':'mM','value':0.00055},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.00057 {1-hydroxymethyl-6-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-6-methylpyrene','units':'mM','value':0.00057},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.00059 {1-hydroxymethylpyrene}','refs':[214],'substrate':'1-hydroxymethylpyrene','units':'mM','value':0.00059},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.00075 {1-hydroxymethylpyrene}','refs':[214],'substrate':'1-hydroxymethylpyrene','units':'mM','value':0.00075},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.0009 {1-formyl-6-methylpyrene}','refs':[214],'substrate':'1-formyl-6-methylpyrene','units':'mM','value':0.0009},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.001 {4-formylpyrene}','refs':[214],'substrate':'4-formylpyrene','units':'mM','value':0.001},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.001 {4-hydroxymethylpyrene}','refs':[214],'substrate':'4-hydroxymethylpyrene','units':'mM','value':0.001},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.00115 {1-hydroxymethyl-6-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-6-methylpyrene','units':'mM','value':0.00115},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.00131 {1-formyl-8-methylpyrene}','refs':[214],'substrate':'1-formyl-8-methylpyrene','units':'mM','value':0.00131},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.00149 {1-formyl-8-methylpyrene}','refs':[214],'substrate':'1-formyl-8-methylpyrene','units':'mM','value':0.00149},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.0021 {2-formylpyrene}','refs':[214],'substrate':'2-formylpyrene','units':'mM','value':0.0021},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.0021 {4-formylpyrene}','refs':[214],'substrate':'4-formylpyrene','units':'mM','value':0.0021},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.0029 {2-formylpyrene}','refs':[214],'substrate':'2-formylpyrene','units':'mM','value':0.0029},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.0038 {1-formyl-6-methylpyrene}','refs':[214],'substrate':'1-formyl-6-methylpyrene','units':'mM','value':0.0038},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.0038 {4-formylpyrene}','refs':[214],'substrate':'4-formylpyrene','units':'mM','value':0.0038},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.0044 {2-hydroxymethylpyrene}','refs':[214],'substrate':'2-hydroxymethylpyrene','units':'mM','value':0.0044},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.0064 {1-hydroxymethyl-6-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-6-methylpyrene','units':'mM','value':0.0064},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.0064 {1-hydroxymethyl-8-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-8-methylpyrene','units':'mM','value':0.0064},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.009 {2-formylpyrene}','refs':[214],'substrate':'2-formylpyrene','units':'mM','value':0.009},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.012 {1-formylpyrene}','refs':[214],'substrate':'1-formylpyrene','units':'mM','value':0.012},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.04 {4-hydroxymethylpyrene}','refs':[214],'substrate':'4-hydroxymethylpyrene','units':'mM','value':0.04},{'comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.059 {1-hydroxymethyl-8-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-8-methylpyrene','units':'mM','value':0.059},{'comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'0.076 {1-hydroxymethylpyrene}','refs':[214],'substrate':'1-hydroxymethylpyrene','units':'mM','value':0.076},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.106 {2-hydroxymethylpyrene}','refs':[214],'substrate':'2-hydroxymethylpyrene','units':'mM','value':0.106},{'chebi':'CHEBI:15343','comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.34 {acetaldehyde}','refs':[214],'substrate':'acetaldehyde','units':'mM','value':0.34},{'comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'0.39 {1-Octanol}','refs':[214],'substrate':'1-Octanol','units':'mM','value':0.39},{'chebi':'CHEBI:16236','comment':'#107# isozyme ADH1C, at 21-23°C <214>','data':'0.77 {ethanol}','refs':[214],'substrate':'ethanol','units':'mM','value':0.77},{'chebi':'CHEBI:15343','comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'26 {acetaldehyde}','refs':[214],'substrate':'acetaldehyde','units':'mM','value':26.0},{'chebi':'CHEBI:16236','comment':'#107# isozyme ADH2, at 21-23°C <214>','data':'33 {ethanol}','refs':[214],'substrate':'ethanol','units':'mM','value':33.0},{'chebi':'CHEBI:17935','comment':'#107# isozyme ADH3, at 21-23°C <214>','data':'9.6 {octanal}','refs':[214],'substrate':'octanal','units':'mM','value':9.6}]),('LO',[{'comment':'#61# 2 isozymes <113>; #24# enzyme polymer forms ''rod-like helical particles <128>','data':'cytosol','refs':[113,128,135,194,214]}]),('MW',[{'comment':'#113# SDS-PAGE <197>; #107# isozyme ADH2, apparent ''molecular weight deduced from electrophoretic ''mobility <214>; #110# isozyme ADH4, calculated ''from amino acid sequence <214>; #93,133# 4 * ''40000, SDS-PAGE <144,239>; #8,10,36,53,80# 2 * ''40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,81,132# ''x * 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, ''ADH-3, SDS-PAGE <49>; #42# 2 * 40000, enzyme form ''ADHI <68>','data':'40000','refs':[11,16,23,24,44,49,52,59,68,87,95,144,197,214,227,239,272]},{'comment':'#107# isozyme ADH3, apparent molecular weight ''deduced from electrophoretic mobility <214>','data':'39500','refs':[214]},{'comment':'#107# isozyme ADH3, calculated from amino acid ''sequence <214>','data':'39720','refs':[214]},{'comment':'#107# isozyme ADH1C, calculated from amino acid ''sequence <214>','data':'39870','refs':[214]},{'comment':'#107# isozyme ADH2, calculated from amino acid ''sequence <214>','data':'40220','refs':[214]},{'comment':'#107# isozyme ADH1C, apparent molecular weight ''deduced from electrophoretic mobility <214>; #110# ''isozyme ADH4, apparent molecular weight deduced ''from electrophoretic mobility <214>','data':'40500','refs':[214]}]),('OSS',[{'comment':'#107,110# DMSO is not an ideal ''substrate-delivering solvent for ADH-catalysed ''reactions <214>; #151# 20% v/v, 24 h, 87% residual ''activity <244>; #56# 20% v/v, 70% residual ''activity <255>','data':'DMSO','refs':[214,244,255]}]),('RE',{'a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,41# ''ordered bi-bi mechanism <31,43>; #4,76# rapid equilibrium ''random mechanism <63>; #8# ordered bi bi mechanism with ''cofactor adding first to form a binary enzyme complex <23>; ''#41# isoenzyme EE and SS: ordered bi bi mechanism <35>; ''#10,33# mechanism is predominantly ordered with ethanol, but ''partially random with butanol <91>; #41# kinetic mechanism is ''random for ethanol oxidation and compulsory ordered for ''acetaldehyde reduction <41>; #38# 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>; #28,68,79# Theorell-Chance mechanism <38,69,74>; #44# ''sequential reaction mechanism <114>; #88# active site ''structure <127>; #79# 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>; #117# ordered bibi ''mechanism, structural and functional implications of amino ''acid residue 47 <110>; #41# ordered sequential bibi reaction ''mechanism, modeling of oxidation kinetic mechanism <117>; ''#119# 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>; #27# the catalytic triad consists of ''Cys44, His67, and Cys154, active site structure <129>)','a secondary alcohol + NAD+ = a ketone + NADH + H+'}),('RN',{'alcohol dehydrogenase'}),('RT',{'redox reaction','reduction','oxidation'}),('SN',{'alcohol:NAD+ oxidoreductase'}),('SP',[{'data':'1-hydroxymethyl-6-methylpyrene + NAD+ = ''1-formyl-6-methylpyrene + NADH + H+ {r}','refs':[214]},{'data':'1-hydroxymethyl-8-methylpyrene + NAD+ = ''1-formyl-8-methylpyrene + NADH + H+ {r}','refs':[214]},{'data':'1-hydroxymethylpyrene + NAD+ = 1-formylpyrene + NADH ''+ H+ {r}','refs':[214]},{'data':'2-hydroxymethylpyrene + NAD+ = 2-formylpyrene + NADH ''+ H+ {r}','refs':[214]},{'data':'4-hydroxymethylpyrene + NAD+ = 4-formylpyrene + NADH ''+ H+ {r}','refs':[214]},{'comment':'#48# best substrate <223>; #79,112# 100% activity ''<61,213>; #101# no activity with NADP+, in reverse ''reaction no activity with NADPH <171>; #31# the ''enzyme is highly specific for ethanol with NAD+ as ''the coenzyme <181>; #113# 88% activity compared to ''cyclohexanol <197>; #107# substrate for isozyme ''ADH1C, extremely poor substrate for isozyme ADH3 ''<214>; #107# substrate for isozyme ADH2 <214>; ''#110# substrate for isozyme ADH4 <214>; #134# the ''enzyme shows a preference for short-chain alcohols ''ethanol and 1-propanol <237>; #155# 12% of the ''activity with butan-1-ol <271>; #161# 33% of the ''activity with 1,4-butanediol <286>) |#120# 83% of ''the activity with butan-2-ol <256>','data':'ethanol + NAD+ = acetaldehyde + NADH + H+','refs':[61,66,79,85,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181,194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233,237,239,246,252,256,271,277,279,284,286,288]},{'comment':'#48# best substrate <223>; #79,112# 100% activity ''<61,213>; #101# no activity with NADP+, in reverse ''reaction no activity with NADPH <171>; #31# the ''enzyme is highly specific for ethanol with NAD+ as ''the coenzyme <181>; #113# 88% activity compared to ''cyclohexanol <197>; #107# substrate for isozyme ''ADH1C, extremely poor substrate for isozyme ADH3 ''<214>; #107# substrate for isozyme ADH2 <214>; ''#110# substrate for isozyme ADH4 <214>; #134# the ''enzyme shows a preference for short-chain alcohols ''ethanol and 1-propanol <237>; #155# 12% of the ''activity with butan-1-ol <271>; #161# 33% of the ''activity with 1,4-butanediol <286>) |#120# 83% of ''the activity with butan-2-ol <256>| {r','data':'ethanol + NAD+ = acetaldehyde + NADH + H+','refs':[61,66,79,85,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181,194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233,237,239,246,252,256,271,277,279,284,286,288]},{'comment':'#13# broad substrate specificity <126>; #10# ''constitutive enzyme <94>; #42# key enzyme in ''ethanol production <68>; #52# one constitutive ''enzyme, ADH-MI and one inducible enzyme, ADH-MII ''<82>; #53# enzyme may be involved in the ''metabolism of dietary wax esters in salmonid fish ''<59>; #79# the enzyme oxidizes alcohols to ''aldehydes or ketones both for detoxification and ''metabolic purposes <38>; #36# involvement in the ''development of male hamster reproductive system ''<47>; #89# 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>; #91# 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>; #61# 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>; #106# the enzyme undergoes a ''substantial conformational change in the apo-holo ''transition, accompanied by loop movements at the ''domain interface <108>; #60# alcohol dehydrogenase ''activity may not limit alcohol supply for ester ''production during ripening <146>; #54# Cm-ADH2 ''cannot reduce branched aldehydes <151>; #10# ''effects of pressure on deuterium isotope effects ''of yeast alcohol dehydrogenase using alternative ''substrates <139>; #93# no activity with methanol ''<144>; #94# the enzyme does not act on short-chain ''normal alkyl alcohols, including methanol and ''ethanol <137>; #97# 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>; #99# 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>; ''#102# 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>; ''#26# when NADH is replaced with NADPH, the ''reaction rate is reduced by 0.6% <188>; #41# ''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>; #113# 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>; #107# ''1-octanal is no substrate for isozyme ADH1C <214>; ''#107# 1-octanal is no substrate for isozyme ADH2 ''<214>; #110# 1-octanal is no substrate for isozyme ''ADH4 <214>; #113# 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>; #122# no activity is ''detected using 1 mM NADP+ <211>; #111# no activity ''towards methanol <210>; #115# substrates are a ''broad range of alkyl alcohols from ethanol to ''1-triacontanol <215>; #124# the physiological ''direction of the catalytic reaction is reduction ''rather than oxidation <219>; #125# 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>; #124# 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>; #128# ''methanol, formaldehyde, and acetone are no ''substrates for HpADH3 <222>; #48# no activity with ''methanol, 1-butanol, glycerol or 2-propanol <223>; ''#129# 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>; #86# the enzyme exhibits broad substrate ''specificity towards aliphatic ketones, ''cycloalkanones, aromatic ketones, and ketoesters ''<226>; #133# 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>; ''#134# the NAD+-dependent HvADH1 shows a preference ''for short-chain alcohols, no activity with ''methanol <237>; #144# broad substrate specificity ''with a preference for the reduction of ketones and ''the oxidation of secondary alcohols <138>; #125# ''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>; #150# enzyme ''reduces aldehydes to (R)-alcohols with more than ''99.8% enantiomeric excess <243>; #151# 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>; #71# ethanol ''dehydrogenase activity of Thermoanaerobium brockii ''is both NAD and NADP linked, reversible, and not ''inhibited by low levels of reaction products ''<103>; #120,143# 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>; #41# 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>; #51# 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>; #153# enzyme is an alcohol dehydrogenase ''with additional activity for all-trans-retinol, ''reaction of EC 1.1.1.184 <272>; #155# 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>; #160# ''the enzyme additionally catalyzes selective ''reduction of 3-quinuclidinone to ''(R)-3-quinuclidinol, with 84% ee and 62% ''conversion after 22 h <274>; #162# Candida ''albicans ADH1 is a bifunctional enzyme that ''catalyzes methylglyoxal oxidation and reduction, ''cf. EC 1.2.1.23 <287>; #161# the enzyme catalyzes ''NAD(H)-dependent oxidation of various alcohols and ''reduction of aldehydes, with a marked preference ''for substrates with functional group at the ''terminal carbon atom <286>; #166# almost no ''activity with D-arabinonate, D-lyxonate, ''D-galactonate, glycerol, meso-erythritol, ''D-ribitol, D-arabitol, D-xylitol, and D-mannitol. ''No activity with propanal, butanal, hexanal, and ''4-oxobutanoic acid <292>; #165# the enzyme ''catalyzes the reduction of acetophenone ''derivatives to the corresponding (S)-chiral ''alcohols in an enantiomerically pure form. The ''substituents on the benzene ring of the aryl ''ketones exert some effect on the enzyme activity, ''although the influence is not dramatic. The ''enantioselectivity of the reduction is not ''affected by the substituents and pattern of the ''substitution. The alpha-chlorinated acetophenone ''shows a much higher activity than the ''unsubstituted one (more than 10 times) <294>','data':'more = ?','refs':[38,47,59,68,82,94,103,105,108,113,118,120,126,137,138,139,144,146,151,156,169,172,180,185,188,197,204,210,211,214,215,218,219,222,223,225,226,237,239,243,244,260,269,271,272,274,275,279,286,287,292,294]},{'comment':'#94# 33% of the activity with 2-propanol, in the ''reverse reaction 435% of the activity with phenyl ''trifluoromethyl ketone <137>; #97# 11% activity ''compared to benzyl alcohol <156>; #99# about 85% ''of activity with ethanol, ADH1 <172>; #113# 57% ''activity compared to cyclohexanol <197>; #107# ''substrate for isozyme ADH3 <214>','data':'1-octanol + NAD+ = octanal + NADH + H+','refs':[137,144,156,172,197,210,214,222,286]},{'comment':'#94# 33% of the activity with 2-propanol, in the ''reverse reaction 435% of the activity with phenyl ''trifluoromethyl ketone <137>; #97# 11% activity ''compared to benzyl alcohol <156>; #99# about 85% ''of activity with ethanol, ADH1 <172>; #113# 57% ''activity compared to cyclohexanol <197>; #107# ''substrate for isozyme ADH3 <214>) {r','data':'1-octanol + NAD+ = octanal + NADH + H+','refs':[137,144,156,172,197,210,214,222,286]}]),('ST',[{'bto':'BTO:0000759','comment':'#5# isoenzyme A2 and B2 <48>; #36# 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>; #107# 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>; #132# class III ADH ''<227>','data':'liver','refs':[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]},{'bto':'BTO:0003833','comment':'#107,110# isozyme ADH4 <214>','data':'buccal mucosa','refs':[214]}]),('SY',[{'comment':'#10,107# isozyme <202,214>','data':'ADH2','refs':[110,123,128,162,170,202,214,215,233,240,252]},{'comment':'#107# isozyme <214>','data':'ADH1C','refs':[214]},{'comment':'#107# isozyme <214>','data':'ADH3','refs':[141,172,177,200,214,252,263]}]),('references',{1:{'info':'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},2:{'info':'Fong, W.P.: Isolation and characterization of ''grass carp (Ctenopharyngodon idellus) liver ''alcohol dehydrogenase. Comp. Biochem. Physiol. B ''(1991) 98, 297-302.'},3:{'info':'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},4:{'info':'Leblova, S.; El Ahmad, M.: Characterization of ''alcohol dehydrogenase isolated from germinating ''bean (Vicia faba) seeds. Collect. Czech. Chem. ''Commun. (1989) 54, 2519-2527.'},5:{'info':'Keung, W.M.; Ho, Y.W.; Fong, W.P.; Lee, C.Y.: ''Isolation and characterization of shrew (Suncus ''murinus) liver alcohol dehydrogenase. Comp. ''Biochem. Physiol. B (1989) 93, 169-173.','pubmed':2666017},6:{'info':'Tong, W.F.; Lin, S.W.: Purification and ''biochemical properties of rice alcohol ''dehydrogenase. Bot. Bull. Acad. Sin. (1988) 29, ''245-253.'},7:{'info':'Van Geyt, J.; Jacobs, M.; Triest, L.: ''Characterization of alcohol dehydrogenase in Najas ''marina L. Aquat. Bot. (1987) 28, 129-141.'},8:{'info':'Vilageliu, L.; Juan, E.; Gonzalez-Duarte, R.: ''Determination of some biochemical features of ''alcohol dehydrogenase from Drosophila ''melanogaster, Drosophila simulans, Drosophila ''virilis, Drosophila funebris, Drosophila imigrans ''and drosophila lebanonensis. Comparison of their ''properties and estimation of the homology of the ''ADH enzyme of different species. Adv. Genet. , ''Dev. , Evol. Drosophila, [Proc. Eur. Drosophila ''Res. Conf. ] (Lakovaara, S. , ed. ) Plenum N. Y. ''(1982) 7, 237-250.'},9:{'info':'Edenberg, H.J.; Brown, C.J.; Carr, L.G.; Ho, W.H.; ''Hu, M.W.: Alcohol dehydrogenase gene expression ''and cloning of the mouse chi-like ADH. Adv. Exp. ''Med. Biol. (1991) 284, 253-262.','pubmed':2053480},10:{'info':'Herrera, E.; Zorzano, A.; Fresneda, V.: ''Comparative kinetics of human and rat liver ''alcohol dehydrogenase. Biochem. Soc. Trans. ''(1983) 11, 729-730.'},11:{'info':'Dafeldecker, W.P.; Vallee, B.L.: Organ-specific ''human alcohol dehydrogenase: isolation and ''characterization of isozymes from testis. ''Biochem. Biophys. Res. Commun. (1986) 134, ''1056-1063.','pubmed':2936344},12:{'info':'Woronick, C.L.: Alcohol dehydrogenase from human ''liver. Methods Enzymol. (1975) 41B, 369-374.','pubmed':236461},13:{'info':'Wagner, F.W.; Burger, A.R.; Vallee, B.L.: Kinetic ''properties of human liver alcohol dehydrogenase: ''oxidation of alcohols by class I isoenzymes. ''Biochemistry (1983) 22, 1857-1863.','pubmed':6342669},14:{'info':'Ditlow, C.C.; Holmquist, B.; Morelock, M.M.; ''Vallee, B.L.: Physical and enzymatic properties ''of a class II alcohol dehydrogenase isozyme of ''human liver: pi-ADH. Biochemistry (1984) 23, ''6363-6368.','pubmed':6397223},15:{'info':'Yin, S.J.; Bosron, W.F.; Magnes, L.J.; Li, T.K.: ''Human liver alcohol dehydrogenase: purification ''and kinetic characterization of the beta 2 beta ''2, beta 2 beta 1, alpha beta 2, and beta 2 gamma ''1 Oriental isoenzymes. Biochemistry (1984) 23, ''5847-5853.','pubmed':6395883},16:{'info':'Wagner, F.W.; Pares, X.; Holmquist, B.; Vallee, ''B.L.: Physical and enzymatic properties of a ''class III isozyme of human liver alcohol ''dehydrogenase: chi-ADH. Biochemistry (1984) 23, ''2193-2199.','pubmed':6375718},17:{'info':'Bosron, W.F.; Magnes, L.J.; Li, T.K.: Kinetic and ''electrophoretic properties of native and ''recombined isoenzymes of human liver alcohol ''dehydrogenase. Biochemistry (1983) 22, 1852-1857.','pubmed':6342668},18:{'info':'Bosron, W.F.; Li, T.K.: Isolation and ''characterization of an anodic form of human liver ''alcohol dehydrogenase. Biochem. Biophys. Res. ''Commun. (1977) 74, 85-91.','pubmed':836289},19:{'info':'Schneider-Bernloehr, H.; Formicka-Kozlowska, G.; ''Buehler, R.; Wartburg, J.P.; Zeppezauer, M.: ''Active-site-specific zinc-depleted and ''reconstituted cobalt(II) human-liver alcohol ''dehydrogenase. Preparation, characterization and ''complexation with NADH and ''trans-4-(N,N-dimethylamino)-cinnamaldehyde. Eur. ''J. Biochem. (1988) 173, 275-280.','pubmed':3360008},20:{'info':'Burnell, J.C.; Li, T.K.; Bosron, W.F.: ''Purification and steady-state kinetic ''characterization of human liver beta 3 beta 3 ''alcohol dehydrogenase. Biochemistry (1989) 28, ''6810-6815.','pubmed':2819035},21:{'info':'Pares, X.; Vallee, B.L.: New human liver alcohol ''dehydrogenase forms with unique kinetic ''characteristics. Biochem. Biophys. Res. Commun. ''(1981) 98, 122-130.','pubmed':7011320},22:{'info':'Bosron, W.F.; Li, T.K.; Vallee, B.L.: New ''molecular forms of human liver alcohol ''dehydrogenase: isolation and characterization of ''ADHIndianapolis. Proc. Natl. Acad. Sci. USA ''(1980) 77, 5784-5788.','pubmed':7003596},23:{'info':'Bosron, W.F.; Li, T.K.; Dafeldecker, W.P.; ''Vallee, B.L.: Human liver pig-alcohol ''dehydrogenase: kinetic and molecular properties. ''Biochemistry (1979) 18, 1101-1105.','pubmed':427099},24:{'info':'Dafeldecker, W.P.; Pares, X.; Vallee, B.L.; ''Bosron, W.F.; Li, T.K.: Simian liver alcohol ''dehydrogenase: isolation and characterization of ''isoenzymes from Saimiri sciureus. Biochemistry ''(1981) 20, 856-861.','pubmed':7011375},25:{'info':'Dafeldecker, W.P.; Meadow, P.E.; Pares, X.; ''Vallee, B.L.: Simian liver alcohol dehydrogenase: ''isolation and characterization of isoenzymes from ''Macaca mulatta. Biochemistry (1981) 20, ''6729-6734.','pubmed':7030395},26:{'info':'Kvassman, J.; Pettersson, G.: Kinetics of ''coenzyme binding to liver alcohol dehydrogenase ''in the pH range 10-12. Eur. J. Biochem. (1987) ''166, 167-172.','pubmed':3595610},27:{'info':'Andersson, L.; Mosbach, K.: Alcohol dehydrogenase ''from horse liver by affinity chromatography. ''Methods Enzymol. (1982) 89, 435-445.','pubmed':6755178},28:{'info':'Pietruszko, R.: Alcohol dehydrogenase from horse ''liver, steroid-active SS isoenzyme. Methods ''Enzymol. (1982) 89, 429-435.'},29:{'info':'Dahl, K.H.; Eklund, H.; McKinley-McKee, J.S.: ''Enantioselective affinity labelling of horse ''liver alcohol dehydrogenase. Correlation of ''inactivation kinetics with the three-dimensional ''structure of the enzyme. Biochem. J. (1983) 211, ''391-396.','pubmed':6347187},30:{'info':'Ramaswamy, S.: Dynamics in alcohol dehydrogenase ''elucidated from crystallographic investigations. ''Adv. Exp. Med. Biol. 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(1984) 106, 3344-3353.'},33:{'info':'Samama, J.P.; Hirsch, D.; Goulas, P.; Biellmann, ''J.F.: Dependence of the substrate specificity and ''kinetic mechanism of horse-liver alcohol ''dehydrogenase on the size of the C-3 pyridinium ''substituent. 3-Benzoylpyridine-adenine ''dinucleotide. Eur. J. Biochem. (1986) 159, ''375-380.','pubmed':3758068},34:{'info':'Eklund, H.: Coenzyme binding in alcohol ''dehydrogenase. Biochem. Soc. Trans. (1989) 17, ''293-296.','pubmed':2753206},35:{'info':'Dworschack, R.T.; Plapp, B.V.: Kinetics of native ''and activated isozymes of horse liver alcohol ''dehydrogenase. Biochemistry (1977) 16, 111-116.','pubmed':831772},36:{'info':'Maret, W.; Andersson, I.; Dietrich, H.; ''Schneider-Bernloehr, H.; Einarsson, R.; ''Zeppezauer, M.: Site-specific substituted ''cobalt(II) horse liver alcohol dehydrogenases. ''Preparation and characterization in solution, ''crystalline and immobilized state. Eur. J. ''Biochem. 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(2018) 8, 1602-1613.'},290:{'info':'Campbell, E.; Wheeldon, I.; Banta, S.: ''Broadening the cofactor specificity of a ''thermostable alcohol dehydrogenase using ''rational protein design introduces novel kinetic ''transient behavior. Biotechnol. Bioeng. (2010) ''107, 763-774.','pubmed':20632378},292:{'info':'Beer, B.; Pick, A.; Doering, M.; Lommes, P.; ''Sieber, V.: Substrate scope of a dehydrogenase ''from Sphingomonas species A1 and its potential ''application in the synthesis of rare sugars and ''sugar derivatives. Microb. Biotechnol. (2018) ''11, 747-758.','pubmed':29697194},293:{'info':'Solanki, K.; Abdallah, W.; Banta, S.: ''Engineering the cofactor specificity of an ''alcohol dehydrogenase via single mutations or '"insertions distal to the 2'-phosphate group of "'NADP(H). Protein Eng. Des. Sel. (2017) 30, ''373-380.','pubmed':28201792},294:{'info':'Zhu, D.; Malik, H.; Hua, L.: Asymmetric ketone ''reduction by a hyperthermophilic alcohol ''dehydrogenase. The substrate specificity, ''enantioselectivity and tolerance of organic ''solvents. Tetrahedron Asymmetry (2006) 17, ''3010-3014.'}}),('tissues',{'BTO:0000759','BTO:0003833'})])──────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────OrderedDict([('protein_id',110),('ec','1.1.1.1'),('organism','Homo sapiens'),('taxonomy',9606),('uniprot','P08319'),('CF',[{'comment':'#13,24,44,61,111,113,166# dependent on ''<113,114,126,128,197,210,292>; #122# specific for ''NAD+ <211>; #162# specific for <287>; #46,96# ''dependent <153,154,159>; #163# preferred cofactor ''<288>; #41# kinetics of coenzyme binding in the ''pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced ''conversion <62>; #41# NAD+ acts as an activator ''which induces an active form of the enzyme <34>; ''#41# preferred substrate <42>; #85# activity with ''mutants G223D/T224I and G223D/T224I/H225N <125>; ''#10# cofactor binding mode <120>; #120# dependent ''on, cofactor binding mechanism and conformation ''from crystal structure analysis <112>; #88# the ''monomer consists of a catalytic and a ''cofactor-binding domain, the cofactor is bound ''between 2 domains in a cleft <127>; ''#7,27,34,50,66# strongly preferred as cofactor ''<135>; #93# specific for NAD+, no activity with ''NADP+, pro-R stereospecificity for hydrogen ''transfer <144>; #99# ADH1 preferrs NAD+ 205fold ''better than NADP+ as cofactor <172>; #15# ADH3 ''does not react with NADP+ <172>; #144# 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>; #112# shows NAD+ as the preferred co-factor ''over NADP+ <213>; #41# 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>; #115# NAD+ is prefered over NADP+ <215>; ''#116# NADP+ is prefered over NAD+ <215>; #125# ''strict requirement for NAD(H) as the coenzyme, no ''activity with NADP+. The specificity constant ''value is 6fold higher for NADH than NAD+ <218>; ''#124# the enzyme transfers the deuteride to the ''Si-face of NAD+ <219>; #48# Adh3 is strictly ''dependent on NAD+/NADH, and shows no activity with ''NADP+/NADPH as cofactor <223>; #134# exclusively ''NAD+ dependent <237>; #51# 57fold preferred over ''NADP+ <279>; #23# H255R single mutant exhibits an ''increased binding affinity toward NADP+ and a ''concomitant reduction in affinity for NAD+ <290>; ''#23# insertion of an RTX domain from the adenylate ''cyclase of Bordetella pertussis into a loop near ''the catalytic active site of the thermostable ''alcohol dehydrogenase D from Pyrococcus furiosus. ''The resultant chimera, beta-AdhD, gains the ''calcium-binding ability of the beta-roll, retains ''the thermostable activity of AdhD, and exhibits ''reduced overall alcohol dehydrogenase activity. ''The addition of calcium to beta-AdhD ''preferentially inhibits NAD+-dependent activity in ''comparison to NADP+-dependent activity. Calcium is ''a competitive inhibitor of AdhD, and the addition ''of the RTX domain introduces calcium-dependent ''noncompetitive inhibition to beta-AdhD affecting ''NAD+-dependent activity <289>','data':'NAD+','refs':[1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74,75,76,77,78,79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98,99,100,101,102,103,105,110,111,112,113,114,115,116,118,120,121,124,125,126,127,128,129,130,135,136,137,138,139,141,143,144,146,148,149,152,153,154,156,157,158,159,161,162,163,164,165,169,172,180,194,195,196,197,198,200,201,202,203,204,205,206,207,208,209,210,211,212,213,214,215,217,218,219,220,221,222,223,225,226,227,229,230,231,232,233,234,237,243,252,254,256,257,260,269,272,279,286,287,288,289,290,292,293]}]),('ID','1.1.1.1'),('IN',[{'comment':'#100# 50% (v/v), 29% loss of activity <173>; #107# ''DMSO inhibits isozyme ADH2-catalysed oxidation in ''an uncompetitive mode and reduction in a mixed ''mode <214>; #107# DMSO inhibits isozymes ''ADH1C-catalysed oxidation in an uncompetitive mode ''and reduction in a mixed mode, no inhibition is ''detected with isozyme ADH3 <214>; #110# DMSO ''inhibits isozymes ADH4-catalysed oxidation in an ''uncompetitive mode and reduction in a mixed mode ''<214>','data':'DMSO','refs':[173,214]},{'comment':'#46# 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>; #36# isoenzyme AA-ADH, BB-ADH and ''TT-ADH <95>; #5# inhibits cell protein ''carbonylation following exposure to crotyl alcohol ''<117>','data':'4-Methylpyrazole','refs':[2,11,14,16,21,23,24,25,95,96,117,135,163,214]},{'comment':'#91# substrate inhibition above 0.5 M <105>; #100# ''50% (v/v), 59% loss of activity <173>; #107# ''ethanol competitively inhibits the oxidation of ''1-hydroxymethylpyrene by ADH1C and ADH3 <214>; ''#110# ethanol competitively inhibits the oxidation ''of 1-hydroxymethylpyrene by ADH4 <214>','data':'ethanol','refs':[105,173,214]}]),('KI',[{'chebi':'CHEBI:16236','comment':'#110# isozyme ADH4, using 1-hydroxymethylpyrene as ''substrate <214>','data':'3.3 {ethanol}','refs':[214],'substrate':'ethanol','units':'mM','value':3.3}]),('KM',[{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.000035 {1-formyl-8-methylpyrene}','refs':[214],'substrate':'1-formyl-8-methylpyrene','units':'mM','value':3.5e-05},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.000036 {1-formyl-6-methylpyrene}','refs':[214],'substrate':'1-formyl-6-methylpyrene','units':'mM','value':3.6e-05},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.00028 {1-hydroxymethyl-6-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-6-methylpyrene','units':'mM','value':0.00028},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.00048 {4-formylpyrene}','refs':[214],'substrate':'4-formylpyrene','units':'mM','value':0.00048},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.00092 {1-formylpyrene}','refs':[214],'substrate':'1-formylpyrene','units':'mM','value':0.00092},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.0016 {1-hydroxymethyl-8-methylpyrene}','refs':[214],'substrate':'1-hydroxymethyl-8-methylpyrene','units':'mM','value':0.0016},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.0029 {4-hydroxymethylpyrene}','refs':[214],'substrate':'4-hydroxymethylpyrene','units':'mM','value':0.0029},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.0069 {2-formylpyrene}','refs':[214],'substrate':'2-formylpyrene','units':'mM','value':0.0069},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.0283 {1-hydroxymethylpyrene}','refs':[214],'substrate':'1-hydroxymethylpyrene','units':'mM','value':0.0283},{'comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'0.033 {2-hydroxymethylpyrene}','refs':[214],'substrate':'2-hydroxymethylpyrene','units':'mM','value':0.033},{'chebi':'CHEBI:15343','comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'12.7 {acetaldehyde}','refs':[214],'substrate':'acetaldehyde','units':'mM','value':12.7},{'chebi':'CHEBI:16236','comment':'#110# isozyme ADH4, at 21-23°C <214>','data':'3.6 {ethanol}','refs':[214],'substrate':'ethanol','units':'mM','value':3.6}]),('LO',[{'comment':'#61# 2 isozymes <113>; #24# enzyme polymer forms ''rod-like helical particles <128>','data':'cytosol','refs':[113,128,135,194,214]}]),('MW',[{'comment':'#113# SDS-PAGE <197>; #107# isozyme ADH2, apparent ''molecular weight deduced from electrophoretic ''mobility <214>; #110# isozyme ADH4, calculated ''from amino acid sequence <214>; #93,133# 4 * ''40000, SDS-PAGE <144,239>; #8,10,36,53,80# 2 * ''40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,81,132# ''x * 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, ''ADH-3, SDS-PAGE <49>; #42# 2 * 40000, enzyme form ''ADHI <68>','data':'40000','refs':[11,16,23,24,44,49,52,59,68,87,95,144,197,214,227,239,272]},{'comment':'#107# isozyme ADH1C, apparent molecular weight ''deduced from electrophoretic mobility <214>; #110# ''isozyme ADH4, apparent molecular weight deduced ''from electrophoretic mobility <214>','data':'40500','refs':[214]}]),('OSS',[{'comment':'#107,110# DMSO is not an ideal ''substrate-delivering solvent for ADH-catalysed ''reactions <214>; #151# 20% v/v, 24 h, 87% residual ''activity <244>; #56# 20% v/v, 70% residual ''activity <255>','data':'DMSO','refs':[214,244,255]}]),('RE',{'a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,41# ''ordered bi-bi mechanism <31,43>; #4,76# rapid equilibrium ''random mechanism <63>; #8# ordered bi bi mechanism with ''cofactor adding first to form a binary enzyme complex <23>; ''#41# isoenzyme EE and SS: ordered bi bi mechanism <35>; ''#10,33# mechanism is predominantly ordered with ethanol, but ''partially random with butanol <91>; #41# kinetic mechanism is ''random for ethanol oxidation and compulsory ordered for ''acetaldehyde reduction <41>; #38# 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>; #28,68,79# Theorell-Chance mechanism <38,69,74>; #44# ''sequential reaction mechanism <114>; #88# active site ''structure <127>; #79# 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>; #117# ordered bibi ''mechanism, structural and functional implications of amino ''acid residue 47 <110>; #41# ordered sequential bibi reaction ''mechanism, modeling of oxidation kinetic mechanism <117>; ''#119# 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>; #27# the catalytic triad consists of ''Cys44, His67, and Cys154, active site structure <129>)','a secondary alcohol + NAD+ = a ketone + NADH + H+'}),('RN',{'alcohol dehydrogenase'}),('RT',{'redox reaction','reduction','oxidation'}),('SN',{'alcohol:NAD+ oxidoreductase'}),('SP',[{'data':'1-hydroxymethyl-6-methylpyrene + NAD+ = ''1-formyl-6-methylpyrene + NADH + H+ {r}','refs':[214]},{'data':'1-hydroxymethyl-8-methylpyrene + NAD+ = ''1-formyl-8-methylpyrene + NADH + H+ {r}','refs':[214]},{'data':'1-hydroxymethylpyrene + NAD+ = 1-formylpyrene + NADH ''+ H+ {r}','refs':[214]},{'data':'2-hydroxymethylpyrene + NAD+ = 2-formylpyrene + NADH ''+ H+ {r}','refs':[214]},{'data':'4-hydroxymethylpyrene + NAD+ = 4-formylpyrene + NADH ''+ H+ {r}','refs':[214]},{'comment':'#48# best substrate <223>; #79,112# 100% activity ''<61,213>; #101# no activity with NADP+, in reverse ''reaction no activity with NADPH <171>; #31# the ''enzyme is highly specific for ethanol with NAD+ as ''the coenzyme <181>; #113# 88% activity compared to ''cyclohexanol <197>; #107# substrate for isozyme ''ADH1C, extremely poor substrate for isozyme ADH3 ''<214>; #107# substrate for isozyme ADH2 <214>; ''#110# substrate for isozyme ADH4 <214>; #134# the ''enzyme shows a preference for short-chain alcohols ''ethanol and 1-propanol <237>; #155# 12% of the ''activity with butan-1-ol <271>; #161# 33% of the ''activity with 1,4-butanediol <286>) |#120# 83% of ''the activity with butan-2-ol <256>','data':'ethanol + NAD+ = acetaldehyde + NADH + H+','refs':[61,66,79,85,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181,194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233,237,239,246,252,256,271,277,279,284,286,288]},{'comment':'#48# best substrate <223>; #79,112# 100% activity ''<61,213>; #101# no activity with NADP+, in reverse ''reaction no activity with NADPH <171>; #31# the ''enzyme is highly specific for ethanol with NAD+ as ''the coenzyme <181>; #113# 88% activity compared to ''cyclohexanol <197>; #107# substrate for isozyme ''ADH1C, extremely poor substrate for isozyme ADH3 ''<214>; #107# substrate for isozyme ADH2 <214>; ''#110# substrate for isozyme ADH4 <214>; #134# the ''enzyme shows a preference for short-chain alcohols ''ethanol and 1-propanol <237>; #155# 12% of the ''activity with butan-1-ol <271>; #161# 33% of the ''activity with 1,4-butanediol <286>) |#120# 83% of ''the activity with butan-2-ol <256>| {r','data':'ethanol + NAD+ = acetaldehyde + NADH + H+','refs':[61,66,79,85,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181,194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233,237,239,246,252,256,271,277,279,284,286,288]},{'comment':'#13# broad substrate specificity <126>; #10# ''constitutive enzyme <94>; #42# key enzyme in ''ethanol production <68>; #52# one constitutive ''enzyme, ADH-MI and one inducible enzyme, ADH-MII ''<82>; #53# enzyme may be involved in the ''metabolism of dietary wax esters in salmonid fish ''<59>; #79# the enzyme oxidizes alcohols to ''aldehydes or ketones both for detoxification and ''metabolic purposes <38>; #36# involvement in the ''development of male hamster reproductive system ''<47>; #89# 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>; #91# 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>; #61# 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>; #106# the enzyme undergoes a ''substantial conformational change in the apo-holo ''transition, accompanied by loop movements at the ''domain interface <108>; #60# alcohol dehydrogenase ''activity may not limit alcohol supply for ester ''production during ripening <146>; #54# Cm-ADH2 ''cannot reduce branched aldehydes <151>; #10# ''effects of pressure on deuterium isotope effects ''of yeast alcohol dehydrogenase using alternative ''substrates <139>; #93# no activity with methanol ''<144>; #94# the enzyme does not act on short-chain ''normal alkyl alcohols, including methanol and ''ethanol <137>; #97# 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>; #99# 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>; ''#102# 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>; ''#26# when NADH is replaced with NADPH, the ''reaction rate is reduced by 0.6% <188>; #41# ''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>; #113# 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>; #107# ''1-octanal is no substrate for isozyme ADH1C <214>; ''#107# 1-octanal is no substrate for isozyme ADH2 ''<214>; #110# 1-octanal is no substrate for isozyme ''ADH4 <214>; #113# 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>; #122# no activity is ''detected using 1 mM NADP+ <211>; #111# no activity ''towards methanol <210>; #115# substrates are a ''broad range of alkyl alcohols from ethanol to ''1-triacontanol <215>; #124# the physiological ''direction of the catalytic reaction is reduction ''rather than oxidation <219>; #125# 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>; #124# 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>; #128# ''methanol, formaldehyde, and acetone are no ''substrates for HpADH3 <222>; #48# no activity with ''methanol, 1-butanol, glycerol or 2-propanol <223>; ''#129# 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>; #86# the enzyme exhibits broad substrate ''specificity towards aliphatic ketones, ''cycloalkanones, aromatic ketones, and ketoesters ''<226>; #133# 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>; ''#134# the NAD+-dependent HvADH1 shows a preference ''for short-chain alcohols, no activity with ''methanol <237>; #144# broad substrate specificity ''with a preference for the reduction of ketones and ''the oxidation of secondary alcohols <138>; #125# ''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>; #150# enzyme ''reduces aldehydes to (R)-alcohols with more than ''99.8% enantiomeric excess <243>; #151# 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>; #71# ethanol ''dehydrogenase activity of Thermoanaerobium brockii ''is both NAD and NADP linked, reversible, and not ''inhibited by low levels of reaction products ''<103>; #120,143# 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>; #41# 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>; #51# 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>; #153# enzyme is an alcohol dehydrogenase ''with additional activity for all-trans-retinol, ''reaction of EC 1.1.1.184 <272>; #155# 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>; #160# ''the enzyme additionally catalyzes selective ''reduction of 3-quinuclidinone to ''(R)-3-quinuclidinol, with 84% ee and 62% ''conversion after 22 h <274>; #162# Candida ''albicans ADH1 is a bifunctional enzyme that ''catalyzes methylglyoxal oxidation and reduction, ''cf. EC 1.2.1.23 <287>; #161# the enzyme catalyzes ''NAD(H)-dependent oxidation of various alcohols and ''reduction of aldehydes, with a marked preference ''for substrates with functional group at the ''terminal carbon atom <286>; #166# almost no ''activity with D-arabinonate, D-lyxonate, ''D-galactonate, glycerol, meso-erythritol, ''D-ribitol, D-arabitol, D-xylitol, and D-mannitol. ''No activity with propanal, butanal, hexanal, and ''4-oxobutanoic acid <292>; #165# the enzyme ''catalyzes the reduction of acetophenone ''derivatives to the corresponding (S)-chiral ''alcohols in an enantiomerically pure form. The ''substituents on the benzene ring of the aryl ''ketones exert some effect on the enzyme activity, ''although the influence is not dramatic. The ''enantioselectivity of the reduction is not ''affected by the substituents and pattern of the ''substitution. The alpha-chlorinated acetophenone ''shows a much higher activity than the ''unsubstituted one (more than 10 times) <294>','data':'more = ?','refs':[38,47,59,68,82,94,103,105,108,113,118,120,126,137,138,139,144,146,151,156,169,172,180,185,188,197,204,210,211,214,215,218,219,222,223,225,226,237,239,243,244,260,269,271,272,274,275,279,286,287,292,294]}]),('ST',[{'bto':'BTO:0003833','comment':'#107,110# isozyme ADH4 <214>','data':'buccal mucosa','refs':[214]}]),('SY',[{'comment':'#110# isozyme <214>','data':'ADH4','refs':[124,174,177,214,252]}]),('references',{1:{'info':'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},2:{'info':'Fong, W.P.: Isolation and characterization of ''grass carp (Ctenopharyngodon idellus) liver ''alcohol dehydrogenase. Comp. Biochem. Physiol. 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Biochemistry (1984) 23, ''6363-6368.','pubmed':6397223},15:{'info':'Yin, S.J.; Bosron, W.F.; Magnes, L.J.; Li, T.K.: ''Human liver alcohol dehydrogenase: purification ''and kinetic characterization of the beta 2 beta ''2, beta 2 beta 1, alpha beta 2, and beta 2 gamma ''1 Oriental isoenzymes. Biochemistry (1984) 23, ''5847-5853.','pubmed':6395883},16:{'info':'Wagner, F.W.; Pares, X.; Holmquist, B.; Vallee, ''B.L.: Physical and enzymatic properties of a ''class III isozyme of human liver alcohol ''dehydrogenase: chi-ADH. Biochemistry (1984) 23, ''2193-2199.','pubmed':6375718},17:{'info':'Bosron, W.F.; Magnes, L.J.; Li, T.K.: Kinetic and ''electrophoretic properties of native and ''recombined isoenzymes of human liver alcohol ''dehydrogenase. Biochemistry (1983) 22, 1852-1857.','pubmed':6342668},18:{'info':'Bosron, W.F.; Li, T.K.: Isolation and ''characterization of an anodic form of human liver ''alcohol dehydrogenase. Biochem. Biophys. Res. ''Commun. 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(2008) 57, 1753-1759.','pubmed':19013301},213:{'info':'Marino-Marmolejo, E.N.; De Leon-Rodriguez, A.; ''de la Rosa, A.P.; Santos, L.: Heterologous ''expression and characterization of an alcohol ''dehydrogenase from the archeon Thermoplasma ''acidophilum. Mol. Biotechnol. (2009) 42, 61-67.','pubmed':19058034},214:{'info':'Kollock, R.; Frank, H.; Seidel, A.; Meinl, W.; ''Glatt, H.: Oxidation of alcohols and reduction ''of aldehydes derived from methyl- and ''dimethylpyrenes by cDNA-expressed human alcohol ''dehydrogenases. Toxicology (2008) 245, 65-75.','pubmed':18242813},215:{'info':'Liu, X.; Dong, Y.; Zhang, J.; Zhang, A.; Wang, ''L.; Feng, L.: Two novel metal-independent ''long-chain alkyl alcohol dehydrogenases from ''Geobacillus thermodenitrificans NG80-2. ''Microbiology (2009) 155, 2078-2085.','pubmed':19383697},217:{'info':'Yanai, H.; Doi, K.; Ohshima, T.: Sulfolobus ''tokodaii ST0053 produces a novel thermostable, ''NAD-dependent medium-chain alcohol ''dehydrogenase. Appl. Environ. Microbiol. (2009) ''75, 1758-1763.','pubmed':19139244},218:{'info':'Pennacchio, A.; Sannino, V.; Sorrentino, G.; ''Rossi, M.; Raia, C.A.; Esposito, L.: Biochemical ''and structural characterization of recombinant ''short-chain NAD(H)-dependent ''dehydrogenase/reductase from Sulfolobus ''acidocaldarius highly enantioselective on diaryl ''diketone benzil. Appl. Microbiol. Biotechnol. ''(2013) 97, 3949-3964.','pubmed':22805786},219:{'info':'Pennacchio, A.; Giordano, A.; Pucci, B.; Rossi, ''M.; Raia, C.A.: Biochemical characterization of ''a recombinant short-chain NAD(H)-dependent ''dehydrogenase/reductase from Sulfolobus ''acidocaldarius. Extremophiles (2010) 14, ''193-204.','pubmed':20049620},220:{'info':'Giordano, A.; Raia, C.A.: Steady-state ''fluorescence properties of S. solfataricus ''alcohol dehydrogenase and its selenomethionyl ''derivative. J. Fluoresc. (2003) 13, 17-24.'},221:{'info':'Giordano, A.; Russo, C.; Raia, C.A.; Kuznetsova, ''I.M.; Stepanenko, O.V.; Turoverov, K.K.: Highly ''UV-absorbing complex in ''selenomethionine-substituted alcohol ''dehydrogenase from Sulfolobus solfataricus. J. ''Proteome Res. (2004) 3, 613-620.','pubmed':15253444},222:{'info':'Suwannarangsee, S.; Kim, S.; Kim, O.C.; Oh, ''D.B.; Seo, J.W.; Kim, C.H.; Rhee, S.K.; Kang, ''H.A.; Chulalaksananukul, W.; Kwon, O.: ''Characterization of alcohol dehydrogenase 3 of ''the thermotolerant methylotrophic yeast ''Hansenula polymorpha. Appl. Microbiol. ''Biotechnol. (2012) 96, 697-709.','pubmed':22249723},223:{'info':'Elleuche, S.; Fodor, K.; Klippel, B.; von der ''Heyde, A.; Wilmanns, M.; Antranikian, G.: ''Structural and biochemical characterisation of a ''NAD+-dependent alcohol dehydrogenase from ''Oenococcus oeni as a new model molecule for ''industrial biotechnology applications. Appl. ''Microbiol. Biotechnol. (2013) 97, 8963-8975.','pubmed':23385476},225:{'info':'Kawano, S.; Yano, M.; Hasegawa, J.; Yasohara, ''Y.: Purification and characterization of an ''NADH-dependent alcohol dehydrogenase from ''Candida maris for the synthesis of optically ''active 1-(pyridyl)ethanol derivatives. Biosci. ''Biotechnol. Biochem. (2011) 75, 1055-1060.','pubmed':21670533},226:{'info':'Zhou, S.; Zhang, S.C.; Lai, D.Y.; Zhang, S.L.; ''Chen, Z.M.: Biocatalytic characterization of a ''short-chain alcohol dehydrogenase with broad ''substrate specificity from thermophilic ''Carboxydothermus hydrogenoformans. Biotechnol. ''Lett. (2013) 35, 359-365.','pubmed':23160740},227:{'info':'Cederlund, E.; Hedlund, J.; Hjelmqvist, L.; ''Jonsson, A.; Shafqat, J.; Norin, A.; Keung, ''W.M.; Persson, B.; Joernvall, H.: ''Characterization of new medium-chain alcohol ''dehydrogenases adds resolution to duplications ''of the class I/III and the sub-class I genes. ''Chem. Biol. Interact. (2011) 191, 8-13.','pubmed':21329683},229:{'info':'Orywal, K.; Jelski, W.; Zdrodowski, M.; ''Szmitkowski, M.: The activity of class I, II, ''III and IV alcohol dehydrogenase isoenzymes and ''aldehyde dehydrogenase in cervical cancer. Clin. ''Biochem. (2011) 44, 1231-1234.','pubmed':21784063},230:{'info':'Kube, J.; Brokamp, C.; Machielsen, R.; van der ''Oost, J.; Maerkl, H.: Influence of temperature ''on the production of an archaeal thermoactive ''alcohol dehydrogenase from Pyrococcus furiosus ''with recombinant Escherichia coli. Extremophiles ''(2006) 10, 221-227.','pubmed':16463078},231:{'info':'Wang, N.; Shi, H.; Yao, Q.; Zhou, Y.; Kang, L.; ''Chen, H.; Chen, K.: Cloning, expression and ''characterization of alcohol dehydrogenases in ''the silkworm Bombyx mori. Genet. Mol. Biol. ''(2011) 34, 240-243.','pubmed':21734824},232:{'info':'Giersberg, M.; Degelmann, A.; Bode, R.; Piontek, ''M.; Kunze, G.: Production of a thermostable ''alcohol dehydrogenase from Rhodococcus ruber in ''three different yeast species using the ''Xplor\x022 transformation/expression platform. ''J. Ind. Microbiol. Biotechnol. (2012) 39, ''1385-1396.','pubmed':22584819},233:{'info':'Komatsu, S.; Deschamps, T.; Thibaut, D.; Hiraga, ''S.; Kato, M.; Chiba, M.; Hashiguchi, A.; Tougou, ''M.; Shimamura, S.; Yasue, H.: Characterization ''of a novel flooding stress-responsive alcohol ''dehydrogenase expressed in soybean roots. Plant ''Mol. Biol. (2011) 77, 309-322.','pubmed':21811849},234:{'info':'Pennacchio, A.; Rossi, M.; Raia, C.A.: Synthesis ''of cinnamyl alcohol from cinnamaldehyde with ''Bacillus stearothermophilus alcohol ''dehydrogenase as the isolated enzyme and in ''recombinant E. coli cells. Appl. Biochem. ''Biotechnol. (2013) 170, 1482-1490.','pubmed':23686507},237:{'info':'Timpson, L.M.; Liliensiek, A.K.; Alsafadi, D.; ''Cassidy, J.; Sharkeym M.A.; Liddell, S.; Allers, ''T.; Paradisi, F.: A comparison of two novel ''alcohol dehydrogenase enzymes (ADH1 and ADH2) ''from the extreme halophile Haloferax volcanii. ''Appl. Microbiol. Biotechnol. (2012) 97, 195-203.','pubmed':22526808},239:{'info':'Hirakawa, H.; Kamiya, N.; Kawarabayashi, Y.; ''Nagamune, T.: Properties of an alcohol ''dehydrogenase from the hyperthermophilic ''archaeon Aeropyrum pernix K1. J. Biosci. Bioeng. ''(2004) 97, 202-206.','pubmed':16233615},243:{'info':'Wu, X.; Zhang, C.; Orita, I.; Imanaka, T.; ''Fukui, T.; Xing, X.H.: Thermostable alcohol ''dehydrogenase from Thermococcus kodakarensis ''KOD1 for enantioselective bioconversion of ''aromatic secondary alcohols. Appl. Environ. ''Microbiol. (2013) 79, 2209-2217.','pubmed':23354700},244:{'info':'Ying, X.; Wang, Y.; Xiong, B.; Wu, T.; Xie, L.; ''Yu, M.; Wang, Z.: Characterization of an ''allylic/benzyl alcohol dehydrogenase from ''Yokenella sp. strain WZY002, an organism ''potentially useful for the synthesis of ''alpha,beta-unsaturated alcohols from allylic ''aldehydes and ketones. Appl. Environ. Microbiol. ''(2014) 80, 2399-2409.','pubmed':24509923},246:{'info':'Kirmair, L.; Seiler, D.L.; Skerra, A.: Stability ''engineering of the Geobacillus ''stearothermophilus alcohol dehydrogenase and ''application for the synthesis of a polyamide 12 ''precursor. Appl. Microbiol. Biotechnol. (2015) ''99, 10501-10513.','pubmed':26329849},252:{'info':'Liang, J.J.; Zhang, M.L.; Ding, M.; Mai, Z.M.; ''Wu, S.X.; Du, Y.; Feng, J.X.: Alcohol ''dehydrogenases from Kluyveromyces marxianus: ''heterologous expression in Escherichia coli and ''biochemical characterization. BMC Biotechnol. ''(2014) 14, 45.','pubmed':24885162},254:{'info':'Kontani, A.; Masuda, M.; Matsumura, H.; ''Nakamura, N.; Yohda, M.; Ohno, H.: A bioanode ''using thermostable alcohol dehydrogenase for an ''ethanol biofuel cell operating at high ''temperatures. Electroanalysis (2014) 26, ''682-686.'},255:{'info':'Willies, S.; Isupov, M.; Littlechild, J.: ''Thermophilic enzymes and their applications in ''biocatalysis: a robust aldo-keto reductase. ''Environ. Technol. (2010) 31, 1159-1167.','pubmed':20718298},256:{'info':'Guagliardi, A.; Martino, M.; Iaccarino, I.; De ''Rosa, M.; Rossi, M.; Bartolucci, S.: ''Purification and characterization of the alcohol ''dehydrogenase from a novel strain of Bacillus ''stearothermophilus growing at 70°C. Int. J. ''Biochem. Cell Biol. (1996) 28, 239-246.','pubmed':8729010},257:{'info':'Meadows, C.W.; Tsang, J.E.; Klinman, J.P.: ''Picosecond-resolved fluorescence studies of ''substrate and cofactor-binding domain mutants in ''a thermophilic alcohol dehydrogenase uncover an ''extended network of communication. J. Am. Chem. ''Soc. (2014) 136, 14821-14833.','pubmed':25314615},260:{'info':'Nagel, Z.D.; Cun, S.; Klinman, J.P.: ''Identification of a long-range protein network ''that modulates active site dynamics in ''extremophilic alcohol dehydrogenases. J. Biol. ''Chem. (2013) 288, 14087-14097.','pubmed':23525111},269:{'info':'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},271:{'info':'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},272:{'info':'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},274:{'info':'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},275:{'info':'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},277:{'info':'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},279:{'info':'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},284:{'info':'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},286:{'info':'Ashraf, R.; Rashid, N.; Kanai, T.; Imanaka, T.; ''Akhtar, M.: Pcal_1311, an alcohol dehydrogenase ''homologue from Pyrobaculum calidifontis, ''displays NADH-dependent high aldehyde reductase ''activity. Extremophiles (2017) 21, 1101-1110.','pubmed':29022135},287:{'info':'Kwak, M.K.; Ku, M.; Kang, S.O.: NAD+-linked ''alcohol dehydrogenase 1 regulates methylglyoxal ''concentration in Candida albicans. FEBS Lett. ''(2014) 588, 1144-1153.','pubmed':24607541},288:{'info':'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},289:{'info':'Abdallah, W.; Solanki, K.; Banta, S.: Insertion ''of a calcium-responsive beta-roll domain into a ''thermostable alcohol dehydrogenase enables ''tunable control over cofactor selectivity. ACS ''Catal. (2018) 8, 1602-1613.'},290:{'info':'Campbell, E.; Wheeldon, I.; Banta, S.: ''Broadening the cofactor specificity of a ''thermostable alcohol dehydrogenase using ''rational protein design introduces novel kinetic ''transient behavior. Biotechnol. Bioeng. (2010) ''107, 763-774.','pubmed':20632378},292:{'info':'Beer, B.; Pick, A.; Doering, M.; Lommes, P.; ''Sieber, V.: Substrate scope of a dehydrogenase ''from Sphingomonas species A1 and its potential ''application in the synthesis of rare sugars and ''sugar derivatives. Microb. Biotechnol. (2018) ''11, 747-758.','pubmed':29697194},293:{'info':'Solanki, K.; Abdallah, W.; Banta, S.: ''Engineering the cofactor specificity of an ''alcohol dehydrogenase via single mutations or '"insertions distal to the 2'-phosphate group of "'NADP(H). Protein Eng. Des. Sel. (2017) 30, ''373-380.','pubmed':28201792},294:{'info':'Zhu, D.; Malik, H.; Hua, L.: Asymmetric ketone ''reduction by a hyperthermophilic alcohol ''dehydrogenase. The substrate specificity, ''enantioselectivity and tolerance of organic ''solvents. Tetrahedron Asymmetry (2006) 17, ''3010-3014.'}}),('tissues',{'BTO:0003833'})])──────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────OrderedDict([('protein_id',8),('ec','1.1.1.1'),('organism','Homo sapiens'),('taxonomy',9606),('uniprot',None),('AP',[{'comment':'#24# 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>','data':'medicine','refs':[123,273]}]),('CF',[{'comment':'#13,24,44,61,111,113,166# dependent on ''<113,114,126,128,197,210,292>; #122# specific for ''NAD+ <211>; #162# specific for <287>; #46,96# ''dependent <153,154,159>; #163# preferred cofactor ''<288>; #41# kinetics of coenzyme binding in the ''pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced ''conversion <62>; #41# NAD+ acts as an activator ''which induces an active form of the enzyme <34>; ''#41# preferred substrate <42>; #85# activity with ''mutants G223D/T224I and G223D/T224I/H225N <125>; ''#10# cofactor binding mode <120>; #120# dependent ''on, cofactor binding mechanism and conformation ''from crystal structure analysis <112>; #88# the ''monomer consists of a catalytic and a ''cofactor-binding domain, the cofactor is bound ''between 2 domains in a cleft <127>; ''#7,27,34,50,66# strongly preferred as cofactor ''<135>; #93# specific for NAD+, no activity with ''NADP+, pro-R stereospecificity for hydrogen ''transfer <144>; #99# ADH1 preferrs NAD+ 205fold ''better than NADP+ as cofactor <172>; #15# ADH3 ''does not react with NADP+ <172>; #144# 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>; #112# shows NAD+ as the preferred co-factor ''over NADP+ <213>; #41# 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>; #115# NAD+ is prefered over NADP+ <215>; ''#116# NADP+ is prefered over NAD+ <215>; #125# ''strict requirement for NAD(H) as the coenzyme, no ''activity with NADP+. The specificity constant ''value is 6fold higher for NADH than NAD+ <218>; ''#124# the enzyme transfers the deuteride to the ''Si-face of NAD+ <219>; #48# Adh3 is strictly ''dependent on NAD+/NADH, and shows no activity with ''NADP+/NADPH as cofactor <223>; #134# exclusively ''NAD+ dependent <237>; #51# 57fold preferred over ''NADP+ <279>; #23# H255R single mutant exhibits an ''increased binding affinity toward NADP+ and a ''concomitant reduction in affinity for NAD+ <290>; ''#23# insertion of an RTX domain from the adenylate ''cyclase of Bordetella pertussis into a loop near ''the catalytic active site of the thermostable ''alcohol dehydrogenase D from Pyrococcus furiosus. ''The resultant chimera, beta-AdhD, gains the ''calcium-binding ability of the beta-roll, retains ''the thermostable activity of AdhD, and exhibits ''reduced overall alcohol dehydrogenase activity. ''The addition of calcium to beta-AdhD ''preferentially inhibits NAD+-dependent activity in ''comparison to NADP+-dependent activity. Calcium is ''a competitive inhibitor of AdhD, and the addition ''of the RTX domain introduces calcium-dependent ''noncompetitive inhibition to beta-AdhD affecting ''NAD+-dependent activity <289>','data':'NAD+','refs':[1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74,75,76,77,78,79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98,99,100,101,102,103,105,110,111,112,113,114,115,116,118,120,121,124,125,126,127,128,129,130,135,136,137,138,139,141,143,144,146,148,149,152,153,154,156,157,158,159,161,162,163,164,165,169,172,180,194,195,196,197,198,200,201,202,203,204,205,206,207,208,209,210,211,212,213,214,215,217,218,219,220,221,222,223,225,226,227,229,230,231,232,233,234,237,243,252,254,256,257,260,269,272,279,286,287,288,289,290,292,293]},{'comment':'#129# required <225>; #44,61# dependent on ''<113,114>; #46# dependent <155>; #163# preferred ''cofactor <288>; #41# kinetics of coenzyme binding ''in the pH range 10-12 <26>; #41# preferred ''coenzyme <42>; #85# activity with mutants ''G223D/T224I and G223D/T224I/H225N <125>; #10# ''cofactor binding mode <120>; #125# 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>; #125# ''strict requirement for NAD(H) as the coenzyme, no ''activity with NADPH. The specificity constant ''value is 6fold higher for NADH than NAD+ <218>; ''#124# the specificity constant value is 21-fold ''higher for NADH than NAD+. No activity with ''NADP(H) <219>; #48# 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>; #164# the cofactor NADH ''can be recycled with D-glucose ''dehydrogenase/D-glucose system or in a coupled ''substrate approach using isopropanol as the ''hydrogen donor <291>','data':'NADH','refs':[1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74,75,76,77,78,79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98,99,100,101,102,105,110,113,114,118,120,123,124,125,129,131,132,133,134,137,140,149,151,155,157,158,161,163,169,200,215,217,218,219,222,223,225,226,231,232,233,234,241,246,252,253,256,259,265,269,272,281,285,286,287,288,290,291]}]),('CL',[{'data':'(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)','refs':[115]},{'data':'(class IV enzyme, expression in Escherichia coli)','refs':[53]},{'data':'(expression of ADH1C*2 in Escherichia coli)','refs':[116]},{'data':'(expression of ADH4 in Escherichia coli)','refs':[124]},{'data':'(expression of human ADH1 in an in vitro ''transcription/translation system, N-terminally ''GST-tagged ADH1 in COS cells and in Escherichia coli)','refs':[228]},{'data':'(expression of isozymes in Escherichia coli strain ''BL21)','refs':[119]}]),('CR',[{'data':'(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)','refs':[109]},{'data':'','refs':[12]}]),('EN',[{'comment':'#8# isozyme alphaalpha, altered active site ''structure and inhibitor binding <109>','data':'A93F','refs':[109]},{'comment':'#8# isozyme gamma(2)gamma(2), altered active site ''structure and inhibitor binding <109>','data':'S48T','refs':[109]},{'comment':'#8# isozyme gamma(2)gamma(2), altered active site ''structure and inhibitor binding <109>','data':'V141L','refs':[109]}]),('GS',[{'data':'(100fold purified enzyme is destroyed by freezing)','refs':[12]}]),('ID','1.1.1.1'),('IN',[{'comment':'#46# 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>; #36# isoenzyme AA-ADH, BB-ADH and ''TT-ADH <95>; #5# inhibits cell protein ''carbonylation following exposure to crotyl alcohol ''<117>','data':'4-Methylpyrazole','refs':[2,11,14,16,21,23,24,25,95,96,117,135,163,214]},{'comment':'#102# 1 mM, complete inhibition <185>; #36# mixed ''type inhibition <47>; #93# 1 mM, 38% inhibition ''<144>; #5# inhibition of isoenzyme A2 and C2, no ''inhibition of isoenzyme B2 <48>; #42# 0.2 mM, ''strong inhibition <68>; #26# 1 mM, 6% inhibition ''<188>','data':'1,10-phenanthroline','refs':[2,14,21,24,25,45,47,48,68,69,75,95,144,185,188]},{'comment':'#79# competitive <38>; #89# strong inhibition ''<118>; #8# 0.05 mM, 50% inhibition <10>; #46# ''competitive inhibitor <163>; #79# 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>; #43,80# organism has ''a pyrazole-sensitive isoenzyme and a ''pyrazole-insensitive enzyme <24,25>; #69# ''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>','data':'pyrazole','refs':[10,12,23,24,25,38,45,48,49,60,61,71,94,118,163,212]},{'comment':'#8# dead-end inhibitor to the enzyme-cofactor ''complex, inhibition of oxidation reaction <116>','data':'3-butylthiolan 1-oxide','refs':[116]},{'comment':'#8# competitive against substrate cyclohexanone ''<116>','data':'4-androsten-3,17-dione','refs':[116]},{'data':'4-bromopyrazole','refs':[23]},{'data':'4-cyanopyrazole','refs':[23]},{'data':'4-nitropyrazole','refs':[23]},{'data':'4-octylpyrazole','refs':[12]},{'data':'4-pentylpyrazole','refs':[12,23]},{'data':'4-propylpyrazole','refs':[23]},{'comment':'#8# i.e. 5alpha-dihydrotestosterone, allosteric, ''competitive against substrate cyclohexanone, ''noncompetitive against NAD+ nd ethanol <116>','data':'5alpha-androstan-17beta-ol-3-one','refs':[116]},{'data':'8-Amino-6-methoxyquinoline','refs':[12]},{'comment':'#8# 1 mM, 4.4% inhibition of hepatic allotype ''ADH1B*1/*1 activity, 2.8% inhibition of hepatic ''allotype ADH1B*2/*2 activity <273>','data':'Acetylsalicylate','refs':[273]},{'comment':'#8# inhibits isozyme gamma(2)gamma(2) <109>','data':'N-1-methylheptylformamide','refs':[109]},{'comment':'#8# inhibits isozyme beta(1)beta(1) <109>','data':'N-benzylformamide','refs':[109]},{'comment':'#8# inhibits isozyme alphaalpha, complex structure ''<109>','data':'N-cyclopentyl-N-cyclobutylformamide','refs':[109]},{'comment':'#8# inhibits isozyme beta(1)beta(1) <109>','data':'N-heptylformamide','refs':[109]},{'data':'NADP+','refs':[21]},{'comment':'#8# 0.5 mM, 16% inhibition of hepatic allotype ''ADH1B*1/*1 activity, 6.1% inhibition of hepatic ''allotype ADH1B*2/*2 activity <273>','data':'acetaminophen','refs':[273]},{'comment':'#8# product inhibition <124>','data':'all-trans-retinal','refs':[124]},{'comment':'#8# weak feedback inhibition <124>','data':'all-trans-retinoic acid','refs':[124]},{'comment':'#8# 0.2 mM, 2.5% inhibition of hepatic allotype ''ADH1B*1/*1 activity, 12% inhibition of hepatic ''allotype ADH1B*2/*2 activity <273>','data':'cimetidine','refs':[273]},{'comment':'#8# 1.5 mM, 12% inhibition of hepatic allotype ''ADH1B*1/*1 activity, 31% inhibition of hepatic ''allotype ADH1B*2/*2 activity <273>','data':'salicylate','refs':[273]},{'data':'sulfonic acid','refs':[21]},{'comment':'#8# competitive against retinol, noncompetitive ''against NAD+ <124>','data':'trifluoroethanol','refs':[91,124]},{'comment':'#8# competitive, stabilizes the retinoid ''compounds, elevates the Km values of the ''substrates, most effective at 0.1% w/v <107>; ''#100# 10% (w/v), 89% inhibition <173>; #113# 13% ''relative activity at 10% (v/v) <197>','data':'Tween 80','refs':[107,173,197]},{'comment':'#8# substrate inhibition, competitive against ''retinol, noncompetitive against NADH <124>','data':'Isobutyramide','refs':[124,175]},{'comment':'#26# 1 mM, 31% inhibition <188>; #46# 15 mM, 85% ''inhibition <66>; #61# 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>; #58# 25% ''inhibition at 10.5 mM, 44% inhibition at 21 mM ''<147>; #57# 31% inhibition at 10.5 mM, 92% ''inhibition at 21 mM <147>; #46# loses 30% of its ''activity immediately on addition of EDTA <163>; ''#113# 2.3% relative activity at 10 mM <197>; #125# ''1 mM, 93% of initial activity <219>','data':'EDTA','refs':[14,24,25,66,76,99,113,147,163,188,197,219,223]},{'data':"2,2'-bipyridine",'refs':[14,25]},{'comment':'#46# competitive inhibitor <163>','data':'4-iodopyrazole','refs':[23,163]},{'data':'8-hydroxyquinoline 5-sulfonic acid','refs':[21,24]},{'comment':'#118# Zn2+ chelator and inhibitor of ADH <209>','data':'dipicolinic acid','refs':[21,24,209]},{'comment':'#36# 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>','data':'4-methoxypyrazole','refs':[23,45,46,47,49,51,53,91]}]),('KI',[{'comment':'#8# pH 7.3, 37°C, versus cyclohexanone <116>','data':'0.0047 {4-androsten-3,17-dione}','refs':[116],'substrate':'4-androsten-3,17-dione','units':'mM','value':0.0047},{'comment':'#8# pH 7.3, 37°C, versus cyclohexanone <116>','data':'0.0047 {5alpha-androstan-17beta-ol-3-one}','refs':[116],'substrate':'5alpha-androstan-17beta-ol-3-one','units':'mM','value':0.0047},{'comment':'#8# pH 7.3, 37°C, versus ethanol <116>','data':'0.014 {5alpha-androstan-17beta-ol-3-one}','refs':[116],'substrate':'5alpha-androstan-17beta-ol-3-one','units':'mM','value':0.014},{'comment':'#8# pH 7.3, 37°C, versus NAD+ <116>','data':'0.028 {5alpha-androstan-17beta-ol-3-one}','refs':[116],'substrate':'5alpha-androstan-17beta-ol-3-one','units':'mM','value':0.028},{'comment':'#8# inhibition kinetics <116>','data':'-999 {more}','refs':[116,123,124],'units':'mM'}]),('KM',[{'comment':'#41,71# kinetics <117,121>; #10# pH-dependence of ''Km-value <89>; #4,76# kinetics of ethanol ''oxidation <63>; #41# kinetics of native and ''modified enzyme with coenzyme analogues <54>; #41# ''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>; #119# detailed kinetic mechanism, ''steady-state kinetics for wild-type and mutant ''enzymes, investigation of pH-dependency <111>; ''#79# 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>; ''#86,91,163# Michaelis-Menten kinetics ''<105,226,288>; #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>; #23# kinetic data füor ''wild-type enzyme and chimeric enzyme created by ''insertion of an RTX domain from the adenylate ''cyclase of Bordetella pertussis into a loop near ''the catalytic active site of the thermostable ''alcohol dehydrogenase D (AdhD) from Pyrococcus ''furiosus <289>','data':'-999 {more}','refs':[13,22,23,31,54,63,75,83,89,105,111,115,116,117,119,120,121,124,130,141,226,288,289],'units':'mM'},{'chebi':'CHEBI:16236','comment':'#8# recombinant allozyme Val308, pH 7.5, 25°C ''<115>','data':'10.6 {ethanol}','refs':[115,135],'substrate':'ethanol','units':'mM','value':10.6},{'chebi':'CHEBI:16908','data':'0.0025 {NADH}','refs':[16],'substrate':'NADH','units':'mM','value':0.0025},{'comment':'#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>','data':'0.0036 {5alpha-androstan-17beta-ol-3-one}','refs':[116],'substrate':'5alpha-androstan-17beta-ol-3-one','units':'mM','value':0.0036},{'comment':'#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>','data':'0.0036 {5beta-pregnan-3,20-dione}','refs':[116],'substrate':'5beta-pregnan-3,20-dione','units':'mM','value':0.0036},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.004 {4-hydroxy-retinol}','refs':[107],'substrate':'4-hydroxy-retinol','units':'mM','value':0.004},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme beta1,beta1 <16>','data':'0.0064 {NADH}','refs':[16],'substrate':'NADH','units':'mM','value':0.0064},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme gamma1,gamma1 <16>','data':'0.007 {NADH}','refs':[16],'substrate':'NADH','units':'mM','value':0.007},{'comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.007 {Octanol}','refs':[14],'substrate':'Octanol','units':'mM','value':0.007},{'chebi':'CHEBI:17987','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.007 {benzyl alcohol}','refs':[14],'substrate':'benzyl alcohol','units':'mM','value':0.007},{'comment':'#8# isoenzyme beta1,beta1 <17>; #8# isoenzyme ''beta2,beta2 <16>','data':'0.0074 {NAD+}','refs':[16,17],'substrate':'NAD+','units':'mM','value':0.0074},{'comment':'#8# isoenzyme gamma1,gamma1 <16,17>','data':'0.0079 {NAD+}','refs':[16,17],'substrate':'NAD+','units':'mM','value':0.0079},{'comment':'#8# isoenzyme alpha,gamma1 <13>','data':'0.008 {Cyclohexanol}','refs':[13],'substrate':'Cyclohexanol','units':'mM','value':0.008},{'comment':'#8# isoenzyme gamma2,gamma2 <16,17>','data':'0.0087 {NAD+}','refs':[16,17],'substrate':'NAD+','units':'mM','value':0.0087},{'comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>','data':'0.009 {Octanol}','refs':[115],'substrate':'Octanol','units':'mM','value':0.009},{'chebi':'CHEBI:17336','data':'0.009 {all-trans-retinol}','refs':[53],'substrate':'all-trans-retinol','units':'mM','value':0.009},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.011 {4-hydroxy-retinol}','refs':[107],'substrate':'4-hydroxy-retinol','units':'mM','value':0.011},{'chebi':'CHEBI:78272','comment':'#8# isozyme ADH1B1, pH 7.5, 25°C <119>','data':'0.011 {9-cis-retinol}','refs':[119],'substrate':'9-cis-retinol','units':'mM','value':0.011},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme alpha,alpha <16>','data':'0.011 {NADH}','refs':[16],'substrate':'NADH','units':'mM','value':0.011},{'chebi':'CHEBI:17898','comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.011 {all-trans-retinal}','refs':[107],'substrate':'all-trans-retinal','units':'mM','value':0.011},{'chebi':'CHEBI:50211','comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>','data':'0.011 {retinol}','refs':[115],'substrate':'retinol','units':'mM','value':0.011},{'chebi':'CHEBI:17898','comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.012 {all-trans-retinal}','refs':[107],'substrate':'all-trans-retinal','units':'mM','value':0.012},{'chebi':'CHEBI:50211','comment':'#8# recombinant allozyme Val308, pH 7.5, 25°C ''<115>','data':'0.012 {retinol}','refs':[115],'substrate':'retinol','units':'mM','value':0.012},{'comment':'#8# isoenzyme alpha,alpha <16,17>','data':'0.013 {NAD+}','refs':[16,17],'substrate':'NAD+','units':'mM','value':0.013},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.015 {4-hydroxy-retinol}','refs':[107],'substrate':'4-hydroxy-retinol','units':'mM','value':0.015},{'comment':'#8# recombinant allozyme Val308, pH 7.5, 25°C ''<115>','data':'0.016 {Octanol}','refs':[115],'substrate':'Octanol','units':'mM','value':0.016},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.017 {4-oxo-retinal}','refs':[107],'substrate':'4-oxo-retinal','units':'mM','value':0.017},{'chebi':'CHEBI:16302','comment':'#8# isozyme ADH1B2, pH 7.5, 25°C <119>','data':'0.018 {11-cis-retinol}','refs':[119],'substrate':'11-cis-retinol','units':'mM','value':0.018},{'data':'0.022 {NAD+}','refs':[12],'substrate':'NAD+','units':'mM','value':0.022},{'chebi':'CHEBI:78272','comment':'#8# isozyme ADH1B2, pH 7.5, 25°C <119>','data':'0.023 {9-cis-retinol}','refs':[119],'substrate':'9-cis-retinol','units':'mM','value':0.023},{'chebi':'CHEBI:17336','comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.023 {all-trans-retinol}','refs':[107],'substrate':'all-trans-retinol','units':'mM','value':0.023},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.024 {3,4-dihydro-retinol}','refs':[107],'substrate':'3,4-dihydro-retinol','units':'mM','value':0.024},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.025 {3,4-dihydro-retinal}','refs':[107],'substrate':'3,4-dihydro-retinal','units':'mM','value':0.025},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.025 {4-oxo-retinal}','refs':[107],'substrate':'4-oxo-retinal','units':'mM','value':0.025},{'data':'0.025 {NAD+}','refs':[16],'substrate':'NAD+','units':'mM','value':0.025},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.026 {3,4-dihydro-retinal}','refs':[107],'substrate':'3,4-dihydro-retinal','units':'mM','value':0.026},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.027 {4-oxo-retinal}','refs':[107],'substrate':'4-oxo-retinal','units':'mM','value':0.027},{'comment':'#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>','data':'0.027 {5beta-Pregnan-3beta-ol-20-one}','refs':[116],'substrate':'5beta-Pregnan-3beta-ol-20-one','units':'mM','value':0.027},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.028 {3,4-dihydro-retinol}','refs':[107],'substrate':'3,4-dihydro-retinol','units':'mM','value':0.028},{'chebi':'CHEBI:88817','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.032 {3-Phenyl-1-propanol}','refs':[14],'substrate':'3-Phenyl-1-propanol','units':'mM','value':0.032},{'chebi':'CHEBI:17336','comment':'#8# isozyme ADH1B2, pH 7.5, 25°C <119>; #8# pH ''7.5, 25°C, isozyme ADH1B2 <107>','data':'0.033 {all-trans-retinol}','refs':[107,119],'substrate':'all-trans-retinol','units':'mM','value':0.033},{'comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.034 {Vanillyl alcohol}','refs':[14],'substrate':'Vanillyl alcohol','units':'mM','value':0.034},{'chebi':'CHEBI:17898','comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.034 {all-trans-retinal}','refs':[107],'substrate':'all-trans-retinal','units':'mM','value':0.034},{'chebi':'CHEBI:16302','comment':'#8# isozyme ADH1B1, pH 7.5, 25°C <119>','data':'0.035 {11-cis-retinol}','refs':[119],'substrate':'11-cis-retinol','units':'mM','value':0.035},{'data':'0.044 {Pentanol}','refs':[96],'substrate':'Pentanol','units':'mM','value':0.044},{'comment':'#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>','data':'0.046 {5beta-androstan-17beta-ol-3-one}','refs':[116],'substrate':'5beta-androstan-17beta-ol-3-one','units':'mM','value':0.046},{'data':'0.047 {12-hydroxydodecanoate}','refs':[96],'substrate':'12-hydroxydodecanoate','units':'mM','value':0.047},{'data':'0.048 {12-hydroxydodecanoate}','refs':[53],'substrate':'12-hydroxydodecanoate','units':'mM','value':0.048},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme beta1,beta1 <17>','data':'0.049 {ethanol}','refs':[15,17],'substrate':'ethanol','units':'mM','value':0.049},{'data':'0.056 {12-Hydroxydodecanoic acid}','refs':[11],'substrate':'12-Hydroxydodecanoic acid','units':'mM','value':0.056},{'comment':'#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>','data':'0.058 {5beta-androstan-3beta-ol-17-one}','refs':[116],'substrate':'5beta-androstan-3beta-ol-17-one','units':'mM','value':0.058},{'chebi':'CHEBI:55329','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.06 {16-hydroxyhexadecanoate}','refs':[14],'substrate':'16-hydroxyhexadecanoate','units':'mM','value':0.06},{'comment':'#8# isoenzyme alpha,gamma1 <13>','data':'0.08 {Octanol}','refs':[13],'substrate':'Octanol','units':'mM','value':0.08},{'chebi':'CHEBI:15343','comment':'#8# isoenzyme beta1,beta1 <15>; #8# isoenzyme ''beta1,beta1, 0.1 M sodium phosphate buffer, pH ''7.5, at 25 °C <20>','data':'0.085 {acetaldehyde}','refs':[15,20],'substrate':'acetaldehyde','units':'mM','value':0.085},{'comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.09 {Pentanol}','refs':[14],'substrate':'Pentanol','units':'mM','value':0.09},{'data':'0.13 {Hexanol}','refs':[53],'substrate':'Hexanol','units':'mM','value':0.13},{'chebi':'CHEBI:17987','data':'0.15 {benzyl alcohol}','refs':[96],'substrate':'benzyl alcohol','units':'mM','value':0.15},{'chebi':'CHEBI:17890','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.2 {tryptophol}','refs':[14],'substrate':'tryptophol','units':'mM','value':0.2},{'comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'0.23 {12-hydroxydodecanoate}','refs':[14],'substrate':'12-hydroxydodecanoate','units':'mM','value':0.23},{'chebi':'CHEBI:15343','comment':'#8# isoenzyme gamma2,gamma2 <15>; #8# isoenzymes ''beta2,beta2 <15>; #8# isoenzyme beta2,beta2, 0.1 M ''sodium phosphate buffer, pH 7.5, 25°C <20>','data':'0.24 {acetaldehyde}','refs':[15,20],'substrate':'acetaldehyde','units':'mM','value':0.24},{'data':'0.24 {butanol}','refs':[96],'substrate':'butanol','units':'mM','value':0.24},{'comment':'#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>','data':'0.25 {5beta-cholanic acid-3-one}','refs':[116],'substrate':'5beta-cholanic acid-3-one','units':'mM','value':0.25},{'data':'0.28 {Pentanol}','refs':[53],'substrate':'Pentanol','units':'mM','value':0.28},{'chebi':'CHEBI:15343','comment':'#8# isoenzyme gamma1,gamma1 <15>','data':'0.33 {acetaldehyde}','refs':[15],'substrate':'acetaldehyde','units':'mM','value':0.33},{'data':'0.34 {NAD+}','refs':[96],'substrate':'NAD+','units':'mM','value':0.34},{'data':'0.55 {1-Octanol}','refs':[11],'substrate':'1-Octanol','units':'mM','value':0.55},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme gamma2,gamma2 <15>','data':'0.63 {ethanol}','refs':[15],'substrate':'ethanol','units':'mM','value':0.63},{'data':'0.79 {butanol}','refs':[53],'substrate':'butanol','units':'mM','value':0.79},{'data':'0.8 {Octanol}','refs':[21],'substrate':'Octanol','units':'mM','value':0.8},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme beta2,beta2, 0.1 M sodium phosphate ''buffer, pH 7.5, 25°C <20>','data':'0.84 {ethanol}','refs':[20],'substrate':'ethanol','units':'mM','value':0.84},{'data':'0.91 {Propanol}','refs':[96],'substrate':'Propanol','units':'mM','value':0.91},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme beta2,beta2 <15>','data':'0.94 {ethanol}','refs':[15],'substrate':'ethanol','units':'mM','value':0.94},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme gamma1,gamma1 <15>','data':'1 {ethanol}','refs':[15],'substrate':'ethanol','units':'mM','value':1.0},{'data':'1.2 {Octanol}','refs':[16],'substrate':'Octanol','units':'mM','value':1.2},{'data':'1.39 {Propanol}','refs':[53],'substrate':'Propanol','units':'mM','value':1.39},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme beta1,beta1 <17>','data':'1.6 {ethanol}','refs':[17],'substrate':'ethanol','units':'mM','value':1.6},{'chebi':'CHEBI:16236','data':'1.8 {ethanol}','refs':[10],'substrate':'ethanol','units':'mM','value':1.8},{'chebi':'CHEBI:17790','data':'10.4 {methanol}','refs':[12],'substrate':'methanol','units':'mM','value':10.4},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme beta2,beta2, 0.1 M sodium phosphate ''buffer, pH 7.5, 25°C <20>','data':'105 {NADH}','refs':[20],'substrate':'NADH','units':'mM','value':105.0},{'data':'11 {Vanillyl alcohol}','refs':[16],'substrate':'Vanillyl alcohol','units':'mM','value':11.0},{'data':'120 {(S)-2-butanol}','refs':[53],'substrate':'(S)-2-butanol','units':'mM','value':120.0},{'chebi':'CHEBI:16236','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'120 {ethanol}','refs':[14],'substrate':'ethanol','units':'mM','value':120.0},{'chebi':'CHEBI:17790','comment':'#8# isoenzyme alpha,gamma1 <13>','data':'150 {methanol}','refs':[13],'substrate':'methanol','units':'mM','value':150.0},{'data':'17 {Hexanol}','refs':[21],'substrate':'Hexanol','units':'mM','value':17.0},{'chebi':'CHEBI:16236','data':'18 {ethanol}','refs':[96],'substrate':'ethanol','units':'mM','value':18.0},{'comment':'#8# isoenzyme beta2,beta2, 0.1 M sodium phosphate ''buffer, pH 7.5, 25°C <20>','data':'180 {NAD+}','refs':[20],'substrate':'NAD+','units':'mM','value':180.0},{'chebi':'CHEBI:17935','data':'2.4 {octanal}','refs':[16],'substrate':'octanal','units':'mM','value':2.4},{'comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'210 {Cyclohexanol}','refs':[14],'substrate':'Cyclohexanol','units':'mM','value':210.0},{'comment':'#8# isoenzyme beta1,beta1 <13>','data':'23 {Cyclohexanol}','refs':[13],'substrate':'Cyclohexanol','units':'mM','value':23.0},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte ''buffer, pH 7.5, 25°C <20>','data':'260 {NADH}','refs':[20],'substrate':'NADH','units':'mM','value':260.0},{'data':'27 {1-Pentanol}','refs':[11],'substrate':'1-Pentanol','units':'mM','value':27.0},{'chebi':'CHEBI:30742','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'290 {ethylene glycol}','refs':[14],'substrate':'ethylene glycol','units':'mM','value':290.0},{'chebi':'CHEBI:15343','comment':'#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte ''buffer, pH 7.5, 25°C <20>','data':'3.4 {acetaldehyde}','refs':[20],'substrate':'acetaldehyde','units':'mM','value':3.4},{'chebi':'CHEBI:28816','comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'310 {2-deoxy-D-ribose}','refs':[14],'substrate':'2-deoxy-D-ribose','units':'mM','value':310.0},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte ''buffer, pH 7.5, 25°C <20>','data':'36 {ethanol}','refs':[20],'substrate':'ethanol','units':'mM','value':36.0},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme alpha,alpha <15,17>','data':'4.2 {ethanol}','refs':[15,17],'substrate':'ethanol','units':'mM','value':4.2},{'chebi':'CHEBI:15343','comment':'#8# isoenzyme alpha,alpha <15>','data':'4.3 {acetaldehyde}','refs':[15],'substrate':'acetaldehyde','units':'mM','value':4.3},{'chebi':'CHEBI:30742','comment':'#8# isoenzyme alpha,gamma1 <13>','data':'50 {ethylene glycol}','refs':[13],'substrate':'ethylene glycol','units':'mM','value':50.0},{'comment':'#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>','data':'560 {2-propanol}','refs':[14],'substrate':'2-propanol','units':'mM','value':560.0},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme beta1,beta1, 0.1 M sodium phosphate ''buffer, pH 7.5, at 25 °C <20>','data':'6.4 {NADH}','refs':[20],'substrate':'NADH','units':'mM','value':6.4},{'comment':'#8# isoenzyme beta1,beta1, 0.1 M sodium phosphate ''buffer, pH 7.5, at 25 °C <20>','data':'7.4 {NAD+}','refs':[20],'substrate':'NAD+','units':'mM','value':7.4},{'comment':'#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte ''buffer, pH 7.5, 25°C <20>','data':'710 {NAD+}','refs':[20],'substrate':'NAD+','units':'mM','value':710.0},{'chebi':'CHEBI:16236','comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>','data':'9 {ethanol}','refs':[115],'substrate':'ethanol','units':'mM','value':9.0},{'chebi':'CHEBI:16236','comment':'#12# pH 10.8 <45>; #128# pH 9.0, 22°C, recombinant ''enzyme <222>','data':'0.45 {ethanol}','refs':[12,45,222],'substrate':'ethanol','units':'mM','value':0.45},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme alpha,alpha <17>; #120# mutant ''C257L, pH 8.0, 60°C <246>','data':'1.5 {ethanol}','refs':[17,246],'substrate':'ethanol','units':'mM','value':1.5},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme gamma1,gamma1 <17>; #122# at pH 7.0 ''and 25°C <211>','data':'3.2 {ethanol}','refs':[17,211],'substrate':'ethanol','units':'mM','value':3.2},{'comment':'#8# isoenzyme beta1,beta1 <16>; #125# 65°C, pH ''10.5 <218>','data':'0.18 {NAD+}','refs':[16,218],'substrate':'NAD+','units':'mM','value':0.18},{'chebi':'CHEBI:16908','comment':'#8# isoenzyme beta2,beta2 <16>; #150# cosubstrate ''acetoin, pH 6.0, 70°C <243>','data':'0.105 {NADH}','refs':[16,243],'substrate':'NADH','units':'mM','value':0.105},{'chebi':'CHEBI:16236','comment':'#16# isoenzyme III <79>; #8# isoenzyme ''alpha,gamma1 <13>; #8# isoenzyme gamma2,gamma2 ''<17>','data':'1.7 {ethanol}','refs':[13,17,79],'substrate':'ethanol','units':'mM','value':1.7},{'comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>; #23# 45°C, pH 8.8, cosubstrate: ''2,3-butanediol, wild-type enzyme <290>','data':'0.063 {NAD+}','refs':[115,290],'substrate':'NAD+','units':'mM','value':0.063},{'chebi':'CHEBI:16236','comment':'#31# 70°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl <181>; ''#8# isoenzyme beta1,beta1, 0.1 M sodium phosphate ''buffer, pH 7.5, at 25 °C <20>','data':'0.022 {ethanol}','refs':[20,181],'substrate':'ethanol','units':'mM','value':0.022},{'chebi':'CHEBI:17336','comment':'#36# isoenzyme BB-ADH <95>; #8# isozyme ADH1B1, pH ''7.5, 25°C <119>; #8# pH 7.5, 25°C, isozyme ADH1B1 ''<107>','data':'0.03 {all-trans-retinol}','refs':[95,107,119],'substrate':'all-trans-retinol','units':'mM','value':0.03},{'chebi':'CHEBI:16236','comment':'#36# isoenzyme TT-ADH <95>','data':'28 {ethanol}','refs':[53,95],'substrate':'ethanol','units':'mM','value':28.0},{'comment':'#55# oxidation of ethanol <99>; #8# recombinant ''allozyme Val308, pH 7.5, 25°C <115>','data':'0.074 {NAD+}','refs':[99,115],'substrate':'NAD+','units':'mM','value':0.074},{'comment':'#9# isoenzyme ADH-1, pH 10.0 <49>','data':'0.1 {12-hydroxydodecanoate}','refs':[16,49],'substrate':'12-hydroxydodecanoate','units':'mM','value':0.1}]),('LO',[{'comment':'#61# 2 isozymes <113>; #24# enzyme polymer forms ''rod-like helical particles <128>','data':'cytosol','refs':[113,128,135,194,214]}]),('ME',[{'comment':'#10# activates <87>; #111# dependent on <210>; ''#46# zinc-containing metalloenzyme <164>; ''#88,117,119# catalytic zinc ion <110,111,127>; ''#106# zinc-containing enzyme <161>; #5# 1 ''catalytic and 1 structural zinc ion per subunit ''<119>; #27# 1 catalytic and 1 structural zinc ion ''per subunit, coordination complex geometry <129>; ''#120# 1 catalytic zinc ion and 1 structural zinc ''ion per enzyme subunit <112>; #44# 1 tightly bound ''ion per subunit <114>; #61# 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>; ''#106# the catalytic active site zinc ion is bound ''to Glu69 in the apoenzyme state, but not in the ''ternary complex state <108>; #95# ADH is a ''putative zinc-dependent alcohol dehydrogenase ''<162>; #46# contains a zinc ion which is directly ''involved in the structural stabilization of enzyme ''molecule <155>; #46# contains eight zinc atoms per ''tetramer <163>; #6# 1 mM ZnSO4, 1.14fold ''activation <169>; #26# 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>; #122# 20% of ''activity is obtained when replacing Mg2+ with 5 mM ''ZnSO4 <211>; #118# contains Zn2+ <209>; #112# ''maximum activity is reached at 0.5 mM Zn2+,Ta1316 ''ADH is able to tolerate high concentrations of ''Zn2+ <213>; #41# zinc metalloenzyme with two zinc ''atoms per subunit <201>; #123# the enzyme likely ''contains 2 Zn2+ <217>; #6# 1 mM, 114% of initial ''activity <169>; #73# 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>; #161# Pcal_1311 is contains two ''zinc atoms per subunit. Twofold increase in enzyme ''activity of Pcal_1311 when produced in the ''presence of 25 microM Zn2+ as compared to the ''protein produced in tap water <286>','data':'Zn2+','refs':[87,104,108,109,110,111,112,113,114,119,120,122,127,129,155,161,162,163,164,169,188,200,201,209,210,211,213,217,241,285,286]},{'comment':'#106# 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>; #80# contains 3.9 gatom of zinc ''per mol of enzyme <24>; #46# 2 mM required for ''optimal activity <66>; #41# substitution of ''catalytic and /or noncatalytic zinc ions by ''cobaltous ions <36>; #41# contains 4 zinc atoms ''per molecule <42>; #8,12# contains 3.8 mol of Zn ''per mol of protein <16,45>; #42# enzyme form ADH I ''and ADH II contain one zinc atom per subunit <67>; ''#14# contains 1 zinc atom per subunit <81>; #36# ''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>; ''#55# contains 1.2 Zn atom per subunit <99>; #68# ''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>; #43# contains 3.7-4.2 mol of zinc per mol of ''enzyme <25>; #104# KmADH3 appears to belong to the ''zinc-containing Adh family <177>; #105# KmADH4 ''appears to belong to the zinc-containing Adh ''family <177>','data':'Zinc','refs':[12,16,19,21,23,24,25,36,42,45,48,49,66,67,69,70,75,81,95,96,99,177,220]}]),('MW',[{'comment':'#113# SDS-PAGE <197>; #107# isozyme ADH2, apparent ''molecular weight deduced from electrophoretic ''mobility <214>; #110# isozyme ADH4, calculated ''from amino acid sequence <214>; #93,133# 4 * ''40000, SDS-PAGE <144,239>; #8,10,36,53,80# 2 * ''40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,81,132# ''x * 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, ''ADH-3, SDS-PAGE <49>; #42# 2 * 40000, enzyme form ''ADHI <68>','data':'40000','refs':[11,16,23,24,44,49,52,59,68,87,95,144,197,214,227,239,272]},{'comment':'#8# ultracentrifugation under non-denaturing ''conditions <23>','data':'78000','refs':[23]},{'comment':'#8# amino acid analysis, ultracentrifugation <18>','data':'78000-85000','refs':[18]},{'comment':'#8# ultracentrifugal analysis <21>','data':'79000-84000','refs':[21]},{'comment':'#8# equilibrium sedimentation <16>','data':'82700','refs':[16]},{'comment':'#70# 4 * 42000, SDS-PAGE <84>; #8# x * 42000, ''SDS-PAGE <14>; #68# 2 * 42000, SDS-PAGE <69>; #8# ''2 * 42000, anodic enzyme form, SDS-PAGE <18>; #69# ''2 * 42000, enzyme form ADH-2 and ADH-3, SDS-PAGE ''<60>; #61# 3 * 42000, ADH I, SDS-PAGE <113>; #23# ''fusion protein, bet-AshD <289>','data':'42000','refs':[14,18,60,69,84,113,289]},{'comment':'#36# 2 * 41000, SDS-PAGE <47>; #8# 2 * 41000, ''class III isoenzyme chi ADH, SDS-PAGE <16>','data':'41000','refs':[16,47]}]),('NSP',[{'comment':'#8# ADH4 might be involved in biosynthesis of ''retinoic acid <124>','data':'all-trans-retinol + NAD+ = all-trans-retinal + NADH','refs':[124,200]},{'comment':'#8# ADH4 might be involved in biosynthesis of ''retinoic acid <124>) {r','data':'all-trans-retinol + NAD+ = all-trans-retinal + NADH','refs':[124,200]},{'comment':'#5# role of the major liver isoenzyme A2 in ''ethanol metabolism <48>; #41# 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>','data':'ethanol + NAD+ = acetaldehyde + NADH','refs':[10,18,21,48,96,102,116,122,141,181]},{'comment':'#5# role of the major liver isoenzyme A2 in ''ethanol metabolism <48>; #41# 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','data':'ethanol + NAD+ = acetaldehyde + NADH','refs':[10,18,21,48,96,102,116,122,141,181]},{'data':'1-butanol + NAD+ = butanal + NADH + H+','refs':[229]},{'data':'1-butanol + NAD+ = butanal + NADH + H+ {r}','refs':[229]},{'data':'isobutyramide + NAD+ = ? {r}','refs':[124]},{'comment':'#10# constitutive enzyme <94>; #42# key enzyme in ''ethanol production <68>; #52# one constitutive ''enzyme, ADH-MI and one inducible enzyme, ADH-MII ''<82>; #53# enzyme may be involved in the ''metabolism of dietary wax esters in salmonid fish ''<59>; #79# the enzyme oxidizes alcohols to ''aldehydes or ketones both for detoxification and ''metabolic purposes <38>; #36# involvement in the ''development of male hamster reproductive system ''<47>; #60# alcohol dehydrogenase activity may not ''limit alcohol supply for ester production during ''ripening <146>; #41# 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>; #113# 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>; #124# the physiological direction of the ''catalytic reaction is reduction rather than ''oxidation <219>','data':'more = ?','refs':[38,47,59,68,82,94,146,180,197,204,219]}]),('PHO',[{'comment':'#5,8# assay at <107,124,200>; #55# reduction of ''acetaldehyde <99>; #3# reduction of substrate <4>; ''#76# and second optimum at pH 9.9 <64>; #46# ''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>','data':'7.5','refs':[4,64,66,99,107,115,122,124,182,196,200,229]},{'comment':'#3# oxidation of substrate <4>; #18# wild-type ''enzyme ADH1-1S <97>; #46# oxidation of benzyl ''alcohol <66>; #8# isoenzyme beta2,beta2 <20>; ''#129# oxidation reaction <225>; #61# assay at, ''forward reaction, ADH I and ADH II <113>; #8# ''isozyme ADH1B2, assay at <119>; #46# mutant enzyme ''N249Y <154>; #8# assay at, total ADH activity ''<229>','data':'8.5','refs':[4,20,66,97,105,113,119,154,225,229]},{'comment':'#119# assay at <111>; #120# oxidation of ethanol ''<256>; #4,72# and a second optimum at pH 9.5 <64>; ''#18# mutant enzyme ADH1-1S1108 <97>; #48# aldehyde ''reduction <223>; #8# assay at, class III enzyme, ''reduction reaction <229>; #133# reduction of ''2-pentanone <239>; #151# oxidation of crotyl ''aclohol <244>','data':'8','refs':[64,97,106,111,215,223,229,239,244,252,256]},{'comment':'#5# assay at <119>; #74# oxidation of ethanol <2>; ''#8# isoenzyme beta1,beta1 <20>; #8# isozyme ''ADH1B1, ADH4, assay at <119>; #123# oxidation of ''1-hexanol <217>; #133# oxidation of 2-pentanol ''<239>','data':'10.5','refs':[2,10,20,119,217,239,284]},{'comment':'#8# and a second optimum at pH 10.0-10.5, ADH ''Indianapolis form 2 and 3 <22>','data':'10-10.5','refs':[22]},{'comment':'#8# acetaldehyde reduction of isoenzyme ''beta2,beta2 <15>','data':'7.4','refs':[15]},{'comment':'#8# assay at, class II enzyme, reduction reaction ''<229>','data':'7.6','refs':[229]},{'comment':'#8# ethanol oxidation, isoenzyme beta2,beta2, ''beta2,beta1, alpha,beta2 and beta2gamma1 <15>','data':'8.5-8.8','refs':[15]},{'comment':'#163# assay at <288>; #164# assay <291>; #8# ''isoenzyme beta3,beta3 <20>; #8# ADH Indianapolis ''form 1 <22>; #123# reduction of benzaldehyde ''<217>; #10# free enzyme, at 25°C <196>','data':'7','refs':[20,22,82,132,196,217,252,288,291]},{'comment':'#12# and a second lower maximum at pH 7.5 <45>','data':'10.8','refs':[12,45]},{'comment':'#8# and a second optimum at pH 10.0-10.5, ADH ''Indianapolis form 2 and 3 <22>; #122# for ethanol ''oxidation <211>','data':'7-7.5','refs':[22,211]},{'comment':'#130# assay at <230>; #42# enzyme form ADH-II, ''oxidation of ethanol <67,68>; #8# standard assay ''at <115>; #125# alcohol oxidation reaction <218>; ''#134# optimally active with 1-butanol at pH 10.0 ''with 4 M KCl <237>; #161# glycine\x96NaOH buffer, ''highest activity for oxidation of ethanol <286>','data':'10','refs':[67,68,75,96,115,118,218,230,237,286]},{'comment':'#8# acetaldehyde reduction, isoenzyme beta1,beta1 ''<15>','data':'5.9','refs':[15,133]},{'comment':'#8,41# assay at <116,117>','data':'7.3','refs':[116,117]},{'comment':'#47# oxidation of 2-phenylethanol <149>','data':'10.4','refs':[14,149]}]),('PHR',[{'comment':'#8# pH 8.0: about 40% of maximal activity, pH ''10.5: about 85% of maximal activity <96>','data':'8-10.5','refs':[96]},{'comment':'#8# about 30% of maximal activity at pH 8.0 and at ''pH 12.0 <14>; #47# pH 8.0: about 50% of maximal ''activity, pH 12.0: about 50% of maximal activity, ''oxidation of 2-phenylethanol <149>; #31# pH 8.0: ''about 70% of maximal activity, pH 12: about 60% of ''maximal activity <181>','data':'8-12','refs':[14,149,181]}]),('PHS',[{'comment':'#8# stable <12>','data':'7-10.6','refs':[12]}]),('PU',[{'data':'(anodic enzyme form)','refs':[18]},{'data':'(class I isoenzymes)','refs':[13]},{'data':'(class II isoenzyme: pi-ADH)','refs':[14]},{'data':'(class III isoenzyme chi-ADH)','refs':[16]},{'data':'(isoenzyme beta3,beta3)','refs':[20]},{'data':'(recombinant ADH2 alloenzymes from Escherichia coli ''by DEAE and AMP or blue Sepharose chromatography, and ''ultrafiltration)','refs':[115]},{'data':'(recombinant enzyme from Escherichia coli by DEAE ion '"exchange, 5'-AMP-resin affinity, and Mono Q ion "'exchange chromatography)','refs':[124]},{'data':'(recombinant isozymes from Escherichia coli strain ''BL21)','refs':[119]},{'data':'','refs':[12,15]}]),('RE',{'a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,41# ''ordered bi-bi mechanism <31,43>; #4,76# rapid equilibrium ''random mechanism <63>; #8# ordered bi bi mechanism with ''cofactor adding first to form a binary enzyme complex <23>; ''#41# isoenzyme EE and SS: ordered bi bi mechanism <35>; ''#10,33# mechanism is predominantly ordered with ethanol, but ''partially random with butanol <91>; #41# kinetic mechanism is ''random for ethanol oxidation and compulsory ordered for ''acetaldehyde reduction <41>; #38# 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>; #28,68,79# Theorell-Chance mechanism <38,69,74>; #44# ''sequential reaction mechanism <114>; #88# active site ''structure <127>; #79# 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>; #117# ordered bibi ''mechanism, structural and functional implications of amino ''acid residue 47 <110>; #41# ordered sequential bibi reaction ''mechanism, modeling of oxidation kinetic mechanism <117>; ''#119# 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>; #27# the catalytic triad consists of ''Cys44, His67, and Cys154, active site structure <129>)','a secondary alcohol + NAD+ = a ketone + NADH + H+'}),('RN',{'alcohol dehydrogenase'}),('RT',{'redox reaction','reduction','oxidation'}),('SA',[{'data':'0.6','refs':[16],'units':'µmol/min/mg','value':0.6},{'data':'0.65','refs':[21],'units':'µmol/min/mg','value':0.65},{'data':'1.47','refs':[14],'units':'µmol/min/mg','value':1.47},{'data':'3.3','refs':[12],'units':'µmol/min/mg','value':3.3},{'comment':'#9# ADH-3 <49>','data':'1.3','refs':[18,49],'units':'µmol/min/mg','value':1.3}]),('SN',{'alcohol:NAD+ oxidoreductase'}),('SP',[{'comment':'#89# 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>; #55# the reduction of ''acetaldehyde is 4.9fold faster than the oxidation ''of ethanol <99>; #52# 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>; #41# ''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>; #119# ''isomerization of the enzyme-NAD+ complex is the ''rate-limiting step for acetaldehyde reduction by ''the wild-type enzyme <111>; #91# 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>; #47# 76% of the activity ''with 2-phenylethanol <149>; #120# proton and ''hydride equivalent transfer in the alcohol ''dehydrogenase enzymatic reaction are modulated by ''the correlated motions between NAD+ and the ''cofactor domain <176>) |#61# acetaldehyde is the ''best substrate for isozyme ADH I <113>','data':'ethanol + NAD+ = acetaldehyde + NADH','refs':[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]},{'comment':'#89# 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>; #55# the reduction of ''acetaldehyde is 4.9fold faster than the oxidation ''of ethanol <99>; #52# 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>; #41# ''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>; #119# ''isomerization of the enzyme-NAD+ complex is the ''rate-limiting step for acetaldehyde reduction by ''the wild-type enzyme <111>; #91# 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>; #47# 76% of the activity ''with 2-phenylethanol <149>; #120# proton and ''hydride equivalent transfer in the alcohol ''dehydrogenase enzymatic reaction are modulated by ''the correlated motions between NAD+ and the ''cofactor domain <176>) |#61# acetaldehyde is the ''best substrate for isozyme ADH I <113>| {r','data':'ethanol + NAD+ = acetaldehyde + NADH','refs':[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]},{'comment':'#10# no activity <87>; #42# very low activity ''<67>; #55# 3% of the activity with ethanol <99>','data':'propan-2-ol + NAD+ = acetone + NADH','refs':[14,43,45,61,64,65,66,67,68,81,84,85,87,90,92,97,99]},{'data':'propanol + NADH = propionaldehyde + NADH','refs':[20,45,53,59,61,65,66,67,68,71,75,77,78,83,84,85,87,90,96,97,99]},{'comment':'#18# no activity <97>; #18# weak activity <75>; ''#41# (R)-2-butanol and (S)-2-butanol <31>','data':'butan-2-ol + NAD+ = butan-2-one + NADH','refs':[20,31,47,53,59,61,64,66,75,83,84,85,92,95,97]},{'comment':'#10# weak <87>; #42# activity with ADH I, no ''activity with ADH II <68>; #42# 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>','data':'butanol + NAD+ = butyraldehyde + NADH','refs':[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]},{'data':'7-cis-retinol + NAD+ = 7-cis-retinal + NADH','refs':[119]},{'comment':'#48# best substrate <223>; #79,112# 100% activity ''<61,213>; #101# no activity with NADP+, in reverse ''reaction no activity with NADPH <171>; #31# the ''enzyme is highly specific for ethanol with NAD+ as ''the coenzyme <181>; #113# 88% activity compared to ''cyclohexanol <197>; #107# substrate for isozyme ''ADH1C, extremely poor substrate for isozyme ADH3 ''<214>; #107# substrate for isozyme ADH2 <214>; ''#110# substrate for isozyme ADH4 <214>; #134# the ''enzyme shows a preference for short-chain alcohols ''ethanol and 1-propanol <237>; #155# 12% of the ''activity with butan-1-ol <271>; #161# 33% of the ''activity with 1,4-butanediol <286>) |#120# 83% of ''the activity with butan-2-ol <256>','data':'ethanol + NAD+ = acetaldehyde + NADH + H+','refs':[61,66,79,85,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181,194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233,237,239,246,252,256,271,277,279,284,286,288]},{'comment':'#48# best substrate <223>; #79,112# 100% activity ''<61,213>; #101# no activity with NADP+, in reverse ''reaction no activity with NADPH <171>; #31# the ''enzyme is highly specific for ethanol with NAD+ as ''the coenzyme <181>; #113# 88% activity compared to ''cyclohexanol <197>; #107# substrate for isozyme ''ADH1C, extremely poor substrate for isozyme ADH3 ''<214>; #107# substrate for isozyme ADH2 <214>; ''#110# substrate for isozyme ADH4 <214>; #134# the ''enzyme shows a preference for short-chain alcohols ''ethanol and 1-propanol <237>; #155# 12% of the ''activity with butan-1-ol <271>; #161# 33% of the ''activity with 1,4-butanediol <286>) |#120# 83% of ''the activity with butan-2-ol <256>| {r','data':'ethanol + NAD+ = acetaldehyde + NADH + H+','refs':[61,66,79,85,103,136,139,140,143,144,147,148,153,159,161,162,163,171,173,174,181,194,195,196,197,203,205,207,208,209,210,211,212,213,214,222,223,231,233,237,239,246,252,256,271,277,279,284,286,288]},{'data':'octanol + NAD+ = octanal + NADH','refs':[110,115,200]},{'comment':'#8# ADH4 might be involved in biosynthesis of ''retinoic acid <124>','data':'all-trans-retinol + NAD+ = all-trans-retinal + NADH','refs':[47,53,93,95,107,119,124,200]},{'comment':'#8# ADH4 might be involved in biosynthesis of ''retinoic acid <124>) {r','data':'all-trans-retinol + NAD+ = all-trans-retinal + NADH','refs':[47,53,93,95,107,119,124,200]},{'comment':'#42# activity with ADH I, no activity with ADH II ''<68>','data':'hexanol + NAD+ = n-hexanal + NADH','refs':[20,21,42,48,53,68,84,92,95,101]},{'comment':'#69# 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>','data':'ethylene glycol + NAD+ = ? + NADH','refs':[13,14,16,48,60,85]},{'data':'11-cis-retinol + NAD+ = 11-cis-retinal + NADH','refs':[93,119]},{'comment':'#5,8# no activity with isozyme ADH1 <119>','data':'13-cis-retinol + NAD+ = 13-cis-retinal + NADH','refs':[93,119]},{'data':'9-cis-retinol + NAD+ = 9-cis-retinal + NADH','refs':[93,119]},{'comment':'#5# oxidized by isoenzyme A2 and B2, no activity ''with isoenzyme C2 <48>','data':'pentanal + NAD+ = pentanone + NADH','refs':[14,16,18,20,24,25,48,53,84,92,96]},{'comment':'#8,18,38,42,69,70# no activity ''<21,60,67,68,75,84,85>; #89# low activity <118>; ''#52# 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>; #80# ''reaction is catalyzed by the pyrazole-sensitive ''enzyme, no activity with the pyrazole-insensitive ''enzyme <24>; #43# 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>; ''#112# 49.9% activity compared to ethanol <213>','data':'methanol + NAD+ = formaldehyde + NADH + H+','refs':[11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,66,67,68,75,82,84,85,101,118,147,171,173,213]},{'comment':'#8,18,38,42,69,70# no activity ''<21,60,67,68,75,84,85>; #89# low activity <118>; ''#52# 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>; #80# ''reaction is catalyzed by the pyrazole-sensitive ''enzyme, no activity with the pyrazole-insensitive ''enzyme <24>; #43# 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>; ''#112# 49.9% activity compared to ethanol <213>) ''{ir','data':'methanol + NAD+ = formaldehyde + NADH + H+','refs':[11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,66,67,68,75,82,84,85,101,118,147,171,173,213]},{'comment':'#8,18,38,42,69,70# no activity ''<21,60,67,68,75,84,85>; #89# low activity <118>; ''#52# 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>; #80# ''reaction is catalyzed by the pyrazole-sensitive ''enzyme, no activity with the pyrazole-insensitive ''enzyme <24>; #43# 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>; ''#112# 49.9% activity compared to ethanol <213>) {r','data':'methanol + NAD+ = formaldehyde + NADH + H+','refs':[11,12,13,14,16,18,20,21,24,25,45,48,49,59,60,66,67,68,75,82,84,85,101,118,147,171,173,213]},{'comment':'#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>','data':'benzyl alcohol + NAD+ = benzaldehyde + NADH','refs':[13,14,16,42,47,48,49,60,66,70,75,96,110,147]},{'comment':'#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','data':'benzyl alcohol + NAD+ = benzaldehyde + NADH','refs':[13,14,16,42,47,48,49,60,66,70,75,96,110,147]},{'comment':'#18# no activity <75>; #5# oxidized by isoenzyme ''A2, no activity with isoenzymes B2 and C2 <48>; ''#43# 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>','data':'cyclohexanol + NAD+ = cyclohexanone + NADH','refs':[13,14,25,47,48,49,60,61,75,77,78,95,101]},{'comment':'#70# weak activity <84>; #42# activity with ADH I, ''no activity with ADH II <68>','data':'octan-1-ol + NAD+ = n-octanal + NADH','refs':[11,13,14,21,25,48,49,60,68,75,84,85,101]},{'comment':'#13# broad substrate specificity <126>; #10# ''constitutive enzyme <94>; #42# key enzyme in ''ethanol production <68>; #52# one constitutive ''enzyme, ADH-MI and one inducible enzyme, ADH-MII ''<82>; #53# enzyme may be involved in the ''metabolism of dietary wax esters in salmonid fish ''<59>; #79# the enzyme oxidizes alcohols to ''aldehydes or ketones both for detoxification and ''metabolic purposes <38>; #36# involvement in the ''development of male hamster reproductive system ''<47>; #89# 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>; #91# 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>; #61# 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>; #106# the enzyme undergoes a ''substantial conformational change in the apo-holo ''transition, accompanied by loop movements at the ''domain interface <108>; #60# alcohol dehydrogenase ''activity may not limit alcohol supply for ester ''production during ripening <146>; #54# Cm-ADH2 ''cannot reduce branched aldehydes <151>; #10# ''effects of pressure on deuterium isotope effects ''of yeast alcohol dehydrogenase using alternative ''substrates <139>; #93# no activity with methanol ''<144>; #94# the enzyme does not act on short-chain ''normal alkyl alcohols, including methanol and ''ethanol <137>; #97# 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>; #99# 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>; ''#102# 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>; ''#26# when NADH is replaced with NADPH, the ''reaction rate is reduced by 0.6% <188>; #41# ''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>; #113# 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>; #107# ''1-octanal is no substrate for isozyme ADH1C <214>; ''#107# 1-octanal is no substrate for isozyme ADH2 ''<214>; #110# 1-octanal is no substrate for isozyme ''ADH4 <214>; #113# 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>; #122# no activity is ''detected using 1 mM NADP+ <211>; #111# no activity ''towards methanol <210>; #115# substrates are a ''broad range of alkyl alcohols from ethanol to ''1-triacontanol <215>; #124# the physiological ''direction of the catalytic reaction is reduction ''rather than oxidation <219>; #125# 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>; #124# 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>; #128# ''methanol, formaldehyde, and acetone are no ''substrates for HpADH3 <222>; #48# no activity with ''methanol, 1-butanol, glycerol or 2-propanol <223>; ''#129# 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>; #86# the enzyme exhibits broad substrate ''specificity towards aliphatic ketones, ''cycloalkanones, aromatic ketones, and ketoesters ''<226>; #133# 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>; ''#134# the NAD+-dependent HvADH1 shows a preference ''for short-chain alcohols, no activity with ''methanol <237>; #144# broad substrate specificity ''with a preference for the reduction of ketones and ''the oxidation of secondary alcohols <138>; #125# ''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>; #150# enzyme ''reduces aldehydes to (R)-alcohols with more than ''99.8% enantiomeric excess <243>; #151# 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>; #71# ethanol ''dehydrogenase activity of Thermoanaerobium brockii ''is both NAD and NADP linked, reversible, and not ''inhibited by low levels of reaction products ''<103>; #120,143# 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>; #41# 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>; #51# 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>; #153# enzyme is an alcohol dehydrogenase ''with additional activity for all-trans-retinol, ''reaction of EC 1.1.1.184 <272>; #155# 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>; #160# ''the enzyme additionally catalyzes selective ''reduction of 3-quinuclidinone to ''(R)-3-quinuclidinol, with 84% ee and 62% ''conversion after 22 h <274>; #162# Candida ''albicans ADH1 is a bifunctional enzyme that ''catalyzes methylglyoxal oxidation and reduction, ''cf. EC 1.2.1.23 <287>; #161# the enzyme catalyzes ''NAD(H)-dependent oxidation of various alcohols and ''reduction of aldehydes, with a marked preference ''for substrates with functional group at the ''terminal carbon atom <286>; #166# almost no ''activity with D-arabinonate, D-lyxonate, ''D-galactonate, glycerol, meso-erythritol, ''D-ribitol, D-arabitol, D-xylitol, and D-mannitol. ''No activity with propanal, butanal, hexanal, and ''4-oxobutanoic acid <292>; #165# the enzyme ''catalyzes the reduction of acetophenone ''derivatives to the corresponding (S)-chiral ''alcohols in an enantiomerically pure form. The ''substituents on the benzene ring of the aryl ''ketones exert some effect on the enzyme activity, ''although the influence is not dramatic. The ''enantioselectivity of the reduction is not ''affected by the substituents and pattern of the ''substitution. The alpha-chlorinated acetophenone ''shows a much higher activity than the ''unsubstituted one (more than 10 times) <294>','data':'more = ?','refs':[38,47,59,68,82,94,103,105,108,113,118,120,126,137,138,139,144,146,151,156,169,172,180,185,188,197,204,210,211,214,215,218,219,222,223,225,226,237,239,243,244,260,269,271,272,274,275,279,286,287,292,294]},{'comment':'#8# substrate of isozyme ADH4 <194>) {r','data':'(2E)-4-hydroxynon-2-enal + NADH + H+ = ''(2E)-non-2-ene-1,4-diol + NAD+','refs':[194]},{'data':'16-hydroxyhexadecanoate + NAD+ = 16-oxohexadecanoic ''acid + NADH','refs':[13,14]},{'data':'17beta-hydroxyetiocholan-3-one + NAD+ = ''ethiocholan-3,17-dione + NADH','refs':[16]},{'data':'2-deoxy-D-ribose + NAD+ = ? + NADH','refs':[14]},{'data':'3,4-dihydro-retinol + NAD+ = 3,4-dihydro-retinal {r}','refs':[107]},{'data':'3-phenyl-1-propanol + NAD+ = 3-phenyl-1-propanone + ''NADH','refs':[13,14]},{'data':'3-pyridylcarbinol + NAD+ = pyridine-3-carbaldehyde + ''NADH','refs':[18]},{'data':'4-hydroxy-retinol + NAD+ = 4-oxo-retinal + NADH {r}','refs':[107]},{'comment':'#8# fluorogenic substrate of class I and II ''isozymes <229>','data':'4-methoxy-1-naphthaldehyde + NAD+ = ''4-methoxy-1-naphthol + NADH + H+','refs':[229]},{'comment':'#8# substrate for class I ADH <180>','data':'4-methoxy-1-naphthaldehyde + NAD+ = ''4-methoxy-1-naphthyl alcohol + NADH + H+','refs':[180]},{'comment':'#8# substrate for class I ADH <206>) {r','data':'4-methoxy-1-naphthaldehyde + NADH + H+ = ''4-methoxynaphthalene-1-carbaldehyde + NAD+','refs':[206]},{'comment':'#8# photometric assay substrate <229>','data':'4-nitrosodimethylaniline + NAD+ = ? + NADH + H+','refs':[229]},{'comment':'#8# low activity <116>','data':'5alpha-pregnan-3beta-ol-20-one + NAD+ = ''5alpha-pregnan-3,20-dione + NADH','refs':[116]},{'comment':'#8# low activity <116>','data':'5beta-cholanic acid-3-one + NADH = 5beta-cholanic ''acid-3-ol + NAD+','refs':[116]},{'data':'5beta-pregnan-3,20-dione + NADH = ?','refs':[116]},{'data':'5beta-pregnan-3beta-ol-20-one + NAD+ = ''5beta-pregnan-3,20-dione + NADH','refs':[116]},{'comment':'#8# substrate for class II ADH <206>) {r','data':'6-methoxy-2-naphthaldehyde + NADH + H+ = ''(6-methoxynaphthalen-2-yl)methanol + NAD+','refs':[206]},{'comment':'#8# substrate for class II ADH <180>','data':'6-methoxy-2-naphthaldehyde + NADH + H+ = ''6-methoxy-2-naphthyl alcohol + NAD+','refs':[180]},{'comment':'#8# class II isozyme, reductive activity <229>','data':'6-methoxy-2-naphthaldehyde + NADH + H+ = ''6-methoxy-2-naphtol + NAD+','refs':[229]},{'data':'digitose + NAD+ = ? + NADH','refs':[16]},{'data':'hexanol + NAD+ = hexanal + NADH','refs':[119]},{'data':'isobutyl alcohol + NAD+ = ? + NADH','refs':[20]},{'data':'isobutyramide + NAD+ = ? {r}','refs':[124]},{'data':'isopentenyl alcohol + NAD+ = isopentanone + NADH','refs':[20]},{'comment':'#8# substrate of class IV ADH <180>','data':'m-nitrobenzaldehyde + NAD+ = m-nitrobenzyl alcohol + ''NADH + H+','refs':[180]},{'data':'n-butanol + NAD+ = butylaldehyde + NADH + H+','refs':[180,206]},{'data':'n-butanol + NAD+ = butylaldehyde + NADH + H+ {r}','refs':[180,206]},{'comment':'#8# substrate of isozyme ADH4 <194>) {r','data':'p-nitrobenzaldehyde + NADH + H+ = p-nitrobenzyl ''alcohol + NAD+','refs':[194]},{'data':'phenylalaninol + NAD+ = ? + NADH','refs':[16]},{'comment':'#8# substrate of isozyme ADH4 <194>) {r','data':'retinal + NADH + H+ = retinol + NAD+','refs':[194]},{'data':'retinol + NAD+ = retinal + NADH','refs':[115]},{'data':'trans-4-(N,N-dimethylamino)-cinnamaldehyde + NADH = ''trans-4-(N,N-dimethylamino)-cinnamyl alcohol + NAD+','refs':[19]},{'data':'tryptophol + NAD+ = ? + NADH','refs':[14]},{'data':'vanillyl alcohol + NAD+ = vanillin + NADH','refs':[14,16]},{'data':'n-butanol + NAD+ = n-butanal + NADH','refs':[120,186]},{'data':'n-butanol + NAD+ = n-butanal + NADH {r}','refs':[120,186]},{'comment':'#97# 100% activity <156>; #47# 199% of the ''activity with 2-phenylethanol <149>; #113# 47% ''activity compared to cyclohexanol <197>; #133# ''i.e. phenylmethanol <239>) |#113# 154% activity ''compared to cyclohexanone <197>; #113# 178% ''activity compared to cyclohexanone <197>; #120# ''33% of the activity with butan-2-ol <256>','data':'benzyl alcohol + NAD+ = benzaldehyde + NADH + H+','refs':[147,149,153,154,156,159,165,180,197,202,205,207,239,256,257,260]},{'comment':'#97# 100% activity <156>; #47# 199% of the ''activity with 2-phenylethanol <149>; #113# 47% ''activity compared to cyclohexanol <197>; #133# ''i.e. phenylmethanol <239>) |#113# 154% activity ''compared to cyclohexanone <197>; #113# 178% ''activity compared to cyclohexanone <197>; #120# ''33% of the activity with butan-2-ol <256>| {r','data':'benzyl alcohol + NAD+ = benzaldehyde + NADH + H+','refs':[147,149,153,154,156,159,165,180,197,202,205,207,239,256,257,260]},{'comment':'#144# 38% of the activity with acetoin <138>','data':'cyclohexanone + NADH + H+ = cyclohexanol + NAD+','refs':[116,138,218]},{'comment':'#144# 38% of the activity with acetoin <138>) {r','data':'cyclohexanone + NADH + H+ = cyclohexanol + NAD+','refs':[116,138,218]},{'comment':'#8# class IV isozyme, reductive activity <229>','data':'3-nitrobenzaldehyde + NADH + H+ = 3-nitrobenzyl ''alcohol + NAD+','refs':[225,229]},{'comment':'#8# class IV isozyme, reductive activity <229>) {r','data':'3-nitrobenzaldehyde + NADH + H+ = 3-nitrobenzyl ''alcohol + NAD+','refs':[225,229]},{'comment':'#97# 30% activity compared to benzyl alcohol ''<156>; #31# 15.7% of the activity with ethanol ''<181>; #99# about 80% of activity with ethanol, ''ADH1 <172>; #113# 142% activity compared to ''cyclohexanol <197>; #112# 67.7% activity compared ''to ethanol <213>','data':'1-butanol + NAD+ = butanal + NADH + H+','refs':[144,147,156,172,181,197,207,210,213,222,223,229,239,286]},{'comment':'#97# 30% activity compared to benzyl alcohol ''<156>; #31# 15.7% of the activity with ethanol ''<181>; #99# about 80% of activity with ethanol, ''ADH1 <172>; #113# 142% activity compared to ''cyclohexanol <197>; #112# 67.7% activity compared ''to ethanol <213>) {r','data':'1-butanol + NAD+ = butanal + NADH + H+','refs':[144,147,156,172,181,197,207,210,213,222,223,229,239,286]},{'data':'(S)-2-butanol + NAD+ = butanone + NADH + H+ {r}','refs':[31,53]},{'comment':'#8# low activity <116>','data':'5beta-androstan-17beta-ol-3-one + NAD+ = ''5beta-androstan-3,17-dione + NADH','refs':[116]},{'data':'5beta-androstan-3beta-ol-17-one + NAD+ = ''5beta-androstan-3,17-dione + NADH','refs':[116]},{'comment':'#70# weak activity <84>; #41# (R)-2-octanol and ''(S)-2-octanol <31>','data':'octan-2-ol + NAD+ = octan-2-one + NADH','refs':[16,31,61,84]},{'comment':'#42# activity with ADH I, no activity with ADH II ''<68>','data':'furfuryl alcohol + NAD+ = furfural + NADH','refs':[16,68]},{'comment':'#42# activity with ADH I, no activity with ADH II ''<68>) {r','data':'furfuryl alcohol + NAD+ = furfural + NADH','refs':[16,68]},{'data':'5alpha-androstan-17beta-ol-3-one + NADH + H+ = ''3beta,17beta-dihydroxy-5alpha-androstan + NAD+','refs':[51,116]},{'comment':'#8# substrate of class IV ADH isozyme <206>','data':'m-nitrobenzaldehyde + NADH + H+ = m-nitrobenzyl ''alcohol + NAD+','refs':[49,206]},{'comment':'#8# substrate of class IV ADH isozyme <206>) {r','data':'m-nitrobenzaldehyde + NADH + H+ = m-nitrobenzyl ''alcohol + NAD+','refs':[49,206]},{'comment':'#42# activity with ADH I, no activity with ADH II ''<68>','data':'pentanol + NAD+ = n-pentanal + NADH','refs':[11,45,49,60,61,68,69,71,75,77,78,85]},{'comment':'#36# oxidized at pH 10, not oxidized at pH 7.5 ''<47>','data':'12-hydroxydodecanoate + NAD+ = 12-oxododecanoic acid ''+ NADH','refs':[11,14,16,47,49,53,60,95,96]},{'data':'octanal + NADH + H+ = octanol + NAD+','refs':[16,49,60]}]),('SS',[{'data':'(4°C, 10 mM HEPES buffer, 1 mM dithioerythritol, pH ''7.5, stable for 2 weeks)','refs':[16]},{'data':'(4°C, 5 mM Na phosphate, pH 7.5, the half-life is 24 ''h. 0.01 mM ethanol effectively stabilizes for several ''weeks)','refs':[18]},{'data':'(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)','refs':[23]},{'data':'(4°C, pH 7.5, stable for 2-3 weeks)','refs':[14]}]),('ST',[{'bto':'BTO:0000759','comment':'#5# isoenzyme A2 and B2 <48>; #36# 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>; #107# 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>; #132# class III ADH ''<227>','data':'liver','refs':[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]},{'bto':'BTO:0000575','comment':'#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>','data':'hepatocyte','refs':[117,186]},{'bto':'BTO:0001175','comment':'#5,8# isozyme ADH4 <119>','data':'retina','refs':[119]},{'bto':'BTO:0001307','comment':'#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>','data':'stomach','refs':[48,49,50,53,96,125,194]},{'bto':'BTO:0000604','data':'adenocarcinoma cell','refs':[229]},{'bto':'BTO:0000135','comment':'#8# the activity of the class I ADH isoenzyme is ''significantly lower in the wall of aortic aneurysm ''than in healthy aorta <206>','data':'aorta','refs':[206]},{'bto':'BTO:0000133','comment':'#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>','data':'blood serum','refs':[150,186]},{'data':'cervical cancer cell','refs':[229]},{'bto':'BTO:0001613','comment':'#8# the total alcohol dehydrogenase activity is ''significantly higher in cancer tissues than in ''healthy colorectum <194>','data':'colorectum','refs':[194]},{'bto':'BTO:0000959','comment':'#8# isozyme ADH4, the total alcohol dehydrogenase ''activity is significantly higher in cancer tissues ''than in healthy esophagus <194>','data':'esophagus','refs':[194]},{'bto':'BTO:0000608','data':'hepatoma cell','refs':[180]},{'bto':'BTO:0001239','data':'serum','refs':[194]},{'bto':'BTO:0001253','data':'skin','refs':[194]},{'bto':'BTO:0000286','comment':'#8# isozyme ADH4 <194>','data':'cornea','refs':[49,194]},{'bto':'BTO:0000671','comment':'#8# isozyme ADH1 <194>; #9# high expression level ''of ADH5 <228>','data':'kidney','refs':[49,194,228]},{'bto':'BTO:0000763','comment':'#8# isozyme ADH1 <194>','data':'lung','refs':[49,194]},{'bto':'BTO:0000988','comment':'#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>','data':'pancreas','refs':[49,191]},{'bto':'BTO:0001424','data':'uterus','refs':[49,229]},{'bto':'BTO:0001363','comment':'#8# the class III enzyme contributes by far the ''bulk of the total alcohol dehydrogenase activity ''<11>; #36# isoenzyme TT-ADH is only found in ''testis <95>; #36# activity increases during the ''prepubertal development <47>','data':'testis','refs':[11,47,49,95]}]),('SU',[{'comment':'#8# x * 42000, SDS-PAGE <14>; #74# x * 28000, ''SDS-PAGE <2>; #1,8,81,132# x * 40000, SDS-PAGE ''<11,44,52,227>; #24# x * 96000, SDS-PAGE <128>; ''#86# x * 30000, SDS-PAGE <226>; #158# x * 85000, ''SDS-PAGE <283>; #14# x * 37500, SDS-PAGE <81>; ''#25# x * 31997, amino acid sequence calculation ''<106>; #99# x * 37443, ADH1, calculated from ''sequence <172>; #15# x * 37983, ADH3, calculated ''from sequence <172>; #31# x * 41300, SDS-PAGE ''<181>; #127# x * 31000, recombinant His6-tagged ''enzyme, SDS-PAGE <231>; #151# x * 36411, ''calculated, x * 37000, SDS-PAGE <244>; #104# x * ''37066, calculated <177>; #105# x * 37311, ''calculated <177>; #73# x * 96000, wild-type, ''SDS-PAGE <241>; #153# x * 40000, SDS-PAGE, x * ''39900, calculated <272>; #158# x * 88000, ''calculated from sequence <283>','data':'?','refs':[2,11,14,44,52,81,106,128,172,177,181,226,227,231,241,244,272,283]},{'comment':'#16# 2 * 45000, SDS-PAGE <79>; #26,79# 2 * 28000, ''SDS-PAGE <61,188>; #67,82# 2 * 58000, SDS-PAGE ''<77,78>; #18# 2 * 35000, SDS-PAGE <75>; #44# 2 * ''38000, SDS-PAGE <114>; #8,10,36,53,80# 2 * 40000, ''SDS-PAGE <16,23,24,59,87,95>; #36# 2 * 41000, ''SDS-PAGE <47>; #68# 2 * 42000, SDS-PAGE <69>; #45# ''2 * 46000, SDS-PAGE <6>; #89# 2 * 43000, SDS-PAGE ''<118>; #12# 2 * 36000, SDS-PAGE <45>; #21,46# 2 * ''37000, SDS-PAGE <66,70,72,165>; #42# 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>; #69# 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>; #42# 2 * ''40000, enzyme form ADHI <68>; #4,72,76# 2 * 27800, ''SDS-PAGE <64>; #42# 2 * 34700, enzyme form ADH-I, ''SDS-PAGE <67>; #3# 2 * 30000 <4>; #42# 2 * 31100, ''enzyme form ADH-II, SDS-PAGE <67>; #61# 2 * 31000, ''ADH II, SDS-PAGE <113>; #106# dimer of dimers, ''X-ray crystallography <161>; #101# 2 * 36900, ''SDS-PAGE <171>; #44# 2 * 38000, recombinant ''enzyme, SDS-PAGE <232>; #73# 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>; #161# 2 * 37555, ''calculated <286>','data':'dimer','refs':[4,6,16,18,21,23,24,45,46,47,48,49,59,60,61,64,66,67,68,69,70,71,72,75,77,78,79,87,95,113,114,118,161,165,171,188,194,205,232,241,284,286]},{'comment':'#27# quaternary organization and stability, ''overview <129>; #8# structure modelling <115>; ''#48# Adh3 forms a Ni2+-containing homodimer in its ''active form, crystal structure analysis, larger ''aggregates are inactive <223>; #125# tetramer ''structure results from chemical crosslinking ''experiments <219>','data':'More','refs':[115,129,219,223]}]),('SY',[{'comment':'#118# mutant enzyme S109P/L116S/Y294C <193>','data':'alcohol dehydrogenase 1','refs':[190,193,212,228]},{'data':'ADH','refs':[108,111,113,115,117,118,119,126,127,129,152,153,154,155,157,158,159,160,161,163,164,194,196,197,199,200,201,203,205,206,207,208,209,211,213,229,231,233,248,251,261,292]},{'data':'ADH1B','refs':[273]},{'data':'ADH1C*1','refs':[116]},{'data':'ADH1C*2','refs':[116]},{'data':'ALDH','refs':[229]},{'data':'aldehyde dehydrogenase','refs':[229]},{'comment':'#8# isoenzyme <206>; #8# isozyme <180>','data':'class I ADH','refs':[180,206,229]},{'comment':'#8# isoenzyme <206>; #8# isozyme <180>','data':'class II ADH','refs':[180,206,229]},{'data':'class III ADH','refs':[229]},{'comment':'#8# isozyme <180>','data':'class IV ADH','refs':[180,229]},{'comment':'#10# isozyme <202>','data':'ADH1','refs':[156,172,202,215,228,252,282,287]},{'comment':'#110# isozyme <214>','data':'ADH4','refs':[124,174,177,214,252]}]),('TN',[{'comment':'#8# turnover-numbers for the class I isoenzymes ''with the substrates ethanol, methanol, ethylene ''glycol, benzyl alcohol, octanol, cyclohexanol and ''16-hydroxyhexadecanoic acid <13>; #41# Km-values ''of active-site Co(II)substituted enzyme <31>; ''#4,76# 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>; #23# kinetic ''data füor wild-type enzyme and chimeric enzyme ''created by insertion of an RTX domain from the ''adenylate cyclase of Bordetella pertussis into a ''loop near the catalytic active site of the ''thermostable alcohol dehydrogenase D (AdhD) from ''Pyrococcus furiosus <289>','data':'-999 {more}','refs':[13,28,31,63,119,141,289],'units':'1/s'},{'chebi':'CHEBI:17898','comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.018 {all-trans-retinal}','refs':[107],'substrate':'all-trans-retinal','units':'1/s','value':0.018},{'chebi':'CHEBI:17336','comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.028 {all-trans-retinol}','refs':[107],'substrate':'all-trans-retinol','units':'1/s','value':0.028},{'comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>','data':'0.038 {Octanol}','refs':[115],'substrate':'Octanol','units':'1/s','value':0.038},{'comment':'#8# recombinant allozyme Val308, pH 7.5, 25°C ''<115>','data':'0.04 {Octanol}','refs':[115],'substrate':'Octanol','units':'1/s','value':0.04},{'chebi':'CHEBI:50211','comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>','data':'0.087 {retinol}','refs':[115],'substrate':'retinol','units':'1/s','value':0.087},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.088 {3,4-dihydro-retinol}','refs':[107],'substrate':'3,4-dihydro-retinol','units':'1/s','value':0.088},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.092 {4-hydroxy-retinol}','refs':[107],'substrate':'4-hydroxy-retinol','units':'1/s','value':0.092},{'chebi':'CHEBI:17790','data':'0.102 {methanol}','refs':[12],'substrate':'methanol','units':'1/s','value':0.102},{'chebi':'CHEBI:50211','comment':'#8# recombinant allozyme Val308, pH 7.5, 25°C ''<115>','data':'0.11 {retinol}','refs':[115],'substrate':'retinol','units':'1/s','value':0.11},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B1 <107>','data':'0.167 {4-oxo-retinal}','refs':[107],'substrate':'4-oxo-retinal','units':'1/s','value':0.167},{'chebi':'CHEBI:16236','comment':'#8# recombinant allozyme Ile308, pH 7.5, 25°C ''<115>','data':'0.167 {ethanol}','refs':[115],'substrate':'ethanol','units':'1/s','value':0.167},{'chebi':'CHEBI:16236','comment':'#8# recombinant allozyme Val308, pH 7.5, 25°C ''<115>','data':'0.175 {ethanol}','refs':[115],'substrate':'ethanol','units':'1/s','value':0.175},{'data':'0.183 {1-Pentanol}','refs':[11],'substrate':'1-Pentanol','units':'1/s','value':0.183},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.22 {3,4-dihydro-retinal}','refs':[107],'substrate':'3,4-dihydro-retinal','units':'1/s','value':0.22},{'data':'0.245 {Pentanol}','refs':[16],'substrate':'Pentanol','units':'1/s','value':0.245},{'chebi':'CHEBI:17336','comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.25 {all-trans-retinol}','refs':[107],'substrate':'all-trans-retinol','units':'1/s','value':0.25},{'data':'0.333 {12-Hydroxydodecanoic acid}','refs':[11],'substrate':'12-Hydroxydodecanoic acid','units':'1/s','value':0.333},{'chebi':'CHEBI:17336','data':'0.4 {all-trans-retinol}','refs':[53],'substrate':'all-trans-retinol','units':'1/s','value':0.4},{'data':'0.467 {Vanillyl alcohol}','refs':[16],'substrate':'Vanillyl alcohol','units':'1/s','value':0.467},{'chebi':'CHEBI:17898','comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'0.55 {all-trans-retinal}','refs':[107],'substrate':'all-trans-retinal','units':'1/s','value':0.55},{'data':'0.583 {Cyclohexanol}','refs':[14],'substrate':'Cyclohexanol','units':'1/s','value':0.583},{'comment':'#8# pH 7.5, anodic enzyme form <18>','data':'0.667 {Pentanol}','refs':[18],'substrate':'Pentanol','units':'1/s','value':0.667},{'comment':'#8# pH 7.5, anodic enzyme form <18>','data':'0.683 {3-Pyridylcarbinol}','refs':[18],'substrate':'3-Pyridylcarbinol','units':'1/s','value':0.683},{'comment':'#8# pH 7.5, anodic enzyme form <18>','data':'0.7 {butanol}','refs':[18],'substrate':'butanol','units':'1/s','value':0.7},{'chebi':'CHEBI:16236','comment':'#8# pH 7.5, anodic enzyme form <18>','data':'0.7 {ethanol}','refs':[18],'substrate':'ethanol','units':'1/s','value':0.7},{'comment':'#8# pH 7.5, anodic enzyme form <18>','data':'0.717 {NAD+}','refs':[18],'substrate':'NAD+','units':'1/s','value':0.717},{'data':'0.75 {2-propanol}','refs':[14],'substrate':'2-propanol','units':'1/s','value':0.75},{'chebi':'CHEBI:30742','data':'0.75 {ethylene glycol}','refs':[14],'substrate':'ethylene glycol','units':'1/s','value':0.75},{'chebi':'CHEBI:17336','comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'0.9 {all-trans-retinol}','refs':[107],'substrate':'all-trans-retinol','units':'1/s','value':0.9},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'1.22 {3,4-dihydro-retinal}','refs':[107],'substrate':'3,4-dihydro-retinal','units':'1/s','value':1.22},{'chebi':'CHEBI:17898','comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'1.83 {all-trans-retinal}','refs':[107],'substrate':'all-trans-retinal','units':'1/s','value':1.83},{'chebi':'CHEBI:17890','data':'1.83 {tryptophol}','refs':[14],'substrate':'tryptophol','units':'1/s','value':1.83},{'chebi':'CHEBI:16236','comment':'#8# pH 10.0, anodic enzyme form <18>','data':'10.2 {ethanol}','refs':[18],'substrate':'ethanol','units':'1/s','value':10.2},{'data':'16 {Pentanol}','refs':[53],'substrate':'Pentanol','units':'1/s','value':16.0},{'data':'17.2 {Propanol}','refs':[53],'substrate':'Propanol','units':'1/s','value':17.2},{'data':'19.5 {Hexanol}','refs':[53],'substrate':'Hexanol','units':'1/s','value':19.5},{'data':'2.17 {(S)-2-butanol}','refs':[53],'substrate':'(S)-2-butanol','units':'1/s','value':2.17},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'2.5 {3,4-dihydro-retinol}','refs':[107],'substrate':'3,4-dihydro-retinol','units':'1/s','value':2.5},{'chebi':'CHEBI:16236','comment':'#8# per active site <12>','data':'2.5 {ethanol}','refs':[12],'substrate':'ethanol','units':'1/s','value':2.5},{'data':'2.83 {1-Octanol}','refs':[11],'substrate':'1-Octanol','units':'1/s','value':2.83},{'chebi':'CHEBI:28816','data':'2.83 {2-deoxy-D-ribose}','refs':[14],'substrate':'2-deoxy-D-ribose','units':'1/s','value':2.83},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'2.83 {4-hydroxy-retinol}','refs':[107],'substrate':'4-hydroxy-retinol','units':'1/s','value':2.83},{'data':'2.95 {12-hydroxydodecanoate}','refs':[53],'substrate':'12-hydroxydodecanoate','units':'1/s','value':2.95},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'20 {4-oxo-retinal}','refs':[107],'substrate':'4-oxo-retinal','units':'1/s','value':20.0},{'data':'3.03 {12-hydroxydodecanoate}','refs':[16],'substrate':'12-hydroxydodecanoate','units':'1/s','value':3.03},{'chebi':'CHEBI:17935','data':'3.33 {octanal}','refs':[16],'substrate':'octanal','units':'1/s','value':3.33},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme gamma1,gamma1 <13>','data':'3.83 {ethanol}','refs':[13],'substrate':'ethanol','units':'1/s','value':3.83},{'chebi':'CHEBI:16236','data':'30.7 {ethanol}','refs':[53],'substrate':'ethanol','units':'1/s','value':30.7},{'comment':'#8# pH 7.5, 25°C, isozyme ADH4 <107>','data':'34.2 {4-hydroxy-retinol}','refs':[107],'substrate':'4-hydroxy-retinol','units':'1/s','value':34.2},{'data':'34.8 {butanol}','refs':[53],'substrate':'butanol','units':'1/s','value':34.8},{'data':'4 {12-hydroxydodecanoate}','refs':[14],'substrate':'12-hydroxydodecanoate','units':'1/s','value':4.0},{'chebi':'CHEBI:16236','comment':'#8# isoenzyme alpha,gamma1 <13>','data':'4 {ethanol}','refs':[13],'substrate':'ethanol','units':'1/s','value':4.0},{'comment':'#8# isoenzyme alpha,gamma1 <13>','data':'4.33 {Octanol}','refs':[13],'substrate':'Octanol','units':'1/s','value':4.33},{'chebi':'CHEBI:17987','comment':'#8# isoenzyme alpha,gamma1 <13>','data':'4.67 {benzyl alcohol}','refs':[13],'substrate':'benzyl alcohol','units':'1/s','value':4.67},{'chebi':'CHEBI:55329','data':'6.17 {16-hydroxyhexadecanoate}','refs':[14],'substrate':'16-hydroxyhexadecanoate','units':'1/s','value':6.17},{'data':'7.33 {Octanol}','refs':[16],'substrate':'Octanol','units':'1/s','value':7.33},{'chebi':'CHEBI:88817','data':'7.5 {3-Phenyl-1-propanol}','refs':[14],'substrate':'3-Phenyl-1-propanol','units':'1/s','value':7.5},{'comment':'#8# pH 7.5, 25°C, isozyme ADH1B2 <107>','data':'7.83 {4-oxo-retinal}','refs':[107],'substrate':'4-oxo-retinal','units':'1/s','value':7.83},{'chebi':'CHEBI:16236','data':'7.83 {ethanol}','refs':[14],'substrate':'ethanol','units':'1/s','value':7.83},{'data':'8 {Pentanol}','refs':[14],'substrate':'Pentanol','units':'1/s','value':8.0},{'data':'8.33 {Octanol}','refs':[14],'substrate':'Octanol','units':'1/s','value':8.33},{'data':'8.67 {Vanillyl alcohol}','refs':[14],'substrate':'Vanillyl alcohol','units':'1/s','value':8.67},{'chebi':'CHEBI:17987','data':'9.17 {benzyl alcohol}','refs':[14],'substrate':'benzyl alcohol','units':'1/s','value':9.17}]),('TO',[{'comment':'#5,8,10# assay at <107,115,119,121,124,229,295>; ''#61# assay at, forward and reverse reaction <113>; ''#10# free enzyme, at 25°C <196>','data':'25','refs':[106,107,113,115,119,121,124,131,196,229,295]},{'comment':'#8,41# assay at <116>','data':'30-37','refs':[116]}]),('TS',[{'comment':'#8# unstable at room temperature and above <12>','data':'23','refs':[12]},{'comment':'#41# distinct subunits have different deactivation ''properties <37>; #10# effect of salts in the high ''concentration range on the thermal stability ''<148>; #41# 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>; #44# temperature ''stability profiles of recombinantly expressed ''enzymes, overview <232>','data':'-999','refs':[37,112,115,148,178,232]}]),('references',{1:{'info':'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},2:{'info':'Fong, W.P.: Isolation and characterization of ''grass carp (Ctenopharyngodon idellus) liver ''alcohol dehydrogenase. Comp. Biochem. Physiol. B ''(1991) 98, 297-302.'},3:{'info':'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},4:{'info':'Leblova, S.; El Ahmad, M.: Characterization of ''alcohol dehydrogenase isolated from germinating ''bean (Vicia faba) seeds. Collect. Czech. Chem. ''Commun. (1989) 54, 2519-2527.'},5:{'info':'Keung, W.M.; Ho, Y.W.; Fong, W.P.; Lee, C.Y.: ''Isolation and characterization of shrew (Suncus ''murinus) liver alcohol dehydrogenase. Comp. ''Biochem. Physiol. B (1989) 93, 169-173.','pubmed':2666017},6:{'info':'Tong, W.F.; Lin, S.W.: Purification and ''biochemical properties of rice alcohol ''dehydrogenase. Bot. Bull. Acad. Sin. (1988) 29, ''245-253.'},7:{'info':'Van Geyt, J.; Jacobs, M.; Triest, L.: ''Characterization of alcohol dehydrogenase in Najas ''marina L. Aquat. Bot. (1987) 28, 129-141.'},8:{'info':'Vilageliu, L.; Juan, E.; Gonzalez-Duarte, R.: ''Determination of some biochemical features of ''alcohol dehydrogenase from Drosophila ''melanogaster, Drosophila simulans, Drosophila ''virilis, Drosophila funebris, Drosophila imigrans ''and drosophila lebanonensis. Comparison of their ''properties and estimation of the homology of the ''ADH enzyme of different species. Adv. Genet. , ''Dev. , Evol. Drosophila, [Proc. Eur. Drosophila ''Res. Conf. ] (Lakovaara, S. , ed. ) Plenum N. Y. ''(1982) 7, 237-250.'},9:{'info':'Edenberg, H.J.; Brown, C.J.; Carr, L.G.; Ho, W.H.; ''Hu, M.W.: Alcohol dehydrogenase gene expression ''and cloning of the mouse chi-like ADH. Adv. Exp. ''Med. Biol. (1991) 284, 253-262.','pubmed':2053480},10:{'info':'Herrera, E.; Zorzano, A.; Fresneda, V.: ''Comparative kinetics of human and rat liver ''alcohol dehydrogenase. Biochem. Soc. Trans. ''(1983) 11, 729-730.'},11:{'info':'Dafeldecker, W.P.; Vallee, B.L.: Organ-specific ''human alcohol dehydrogenase: isolation and ''characterization of isozymes from testis. ''Biochem. Biophys. Res. Commun. (1986) 134, ''1056-1063.','pubmed':2936344},12:{'info':'Woronick, C.L.: Alcohol dehydrogenase from human ''liver. Methods Enzymol. (1975) 41B, 369-374.','pubmed':236461},13:{'info':'Wagner, F.W.; Burger, A.R.; Vallee, B.L.: Kinetic ''properties of human liver alcohol dehydrogenase: ''oxidation of alcohols by class I isoenzymes. ''Biochemistry (1983) 22, 1857-1863.','pubmed':6342669},14:{'info':'Ditlow, C.C.; Holmquist, B.; Morelock, M.M.; ''Vallee, B.L.: Physical and enzymatic properties ''of a class II alcohol dehydrogenase isozyme of ''human liver: pi-ADH. 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