1.1.1.1: alcohol dehydrogenase This is an abbreviated version! For detailed information about alcohol dehydrogenase, go to the full flat file .
Reaction
a primary alcohol +
NAD+ =
an aldehyde +
NADH +
H+
Synonyms (R)-specific alcohol dehydrogenase, 40 kDa allergen, Aadh1, acetaldehyde-alcohol dehydrogenase, ADH, ADH 1, ADH class III, ADH I, ADH II, ADH-10, ADH-A, ADH-A2, ADH-B2, ADH-C2, ADH-HT, ADH-I, ADH1, ADH1B, ADH1C, ADH1C*1, ADH1C*2, Adh1p, ADH2, ADH3, ADH4, ADH5, ADH6Hp, ADH8, AdhA, AdhB, AdhC, AdhD, AdhE, ADHES77, ADS1, AFPDH, alcohol dehydrogenase, alcohol dehydrogenase (NAD), alcohol dehydrogenase 1, alcohol dehydrogenase 10, alcohol dehydrogenase 2, alcohol dehydrogenase 3, alcohol dehydrogenase 5, alcohol dehydrogenase class-P, alcohol dehydrogenase D, alcohol dehydrogenase GroES domain protein, alcohol dehydrogenase I, alcohol dehydrogenase II, Alcohol dehydrogenase-B2, alcohol dependent dehydrogenase, alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent, alcohol:NAD+ oxidoreductase, aldehyde dehydrogenase, aldehyde reductase, aldehyde/alcohol dehydrogenase, ALDH, aliphatic alcohol dehydrogenase, alpha-ketoaldehyde dehydrogenase, anti-Prelog reductase, APE2239, APE_2239.1, ARAD1B16786p, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, bifunctional alcohol/aldehyde dehydrogenase, CHY1186, class I ADH, class I ALDH, class II ADH, class III ADH, class III alcohol dehydrogenase, class IV ADH, Cm-ADH2, Cthe_0423, DADH, dehydrogenase, alcohol, ethanol dehydrogenase, FALDH, FDH, Gastric alcohol dehydrogenase, Glutathione-dependent formaldehyde dehydrogenase, glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase, GSH-FDH, GSH-FDH/ADH, HLAD, hLADH, HpADH3, HtADH, HvADH1, HVO_2428, iron-containing alcohol dehydrogenase, KlADH4, KlDH3, KmADH3, KmADH4, LSADH, medium chain alcohol dehydrogenase, medium-chain NAD+-dependent ADH, medium-chain secondary alcohol dehydrogenase, MGD, More, NAD(H)-dependent alcohol dehydrogenase, NAD+-ADH, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent alcohol dehydrogenase, NAD+-dependent SDR, NAD+-linked alcohol dehydrogenase 1, NAD+-linked methylglyoxal dehydrogenase, NAD-dependent alcohol dehydrogenase, NAD-dependent medium-chain ADH, NAD-specific aromatic alcohol dehydrogenase, NADH-alcohol dehydrogenase, NADH-aldehyde dehydrogenase, NADH-dependent alcohol dehydrogenase, NADH-dependent anti-Prelog specific ADH, NADH:p-NTF-reductase, Octanol dehydrogenase, Pcal_1311, PF0991 protein, PF1960, PFADH, primary alcohol dehydrogenase, Retinol dehydrogenase, SaADH, SaADH2, Saci_1232, SADH, SCAD, sec-ADH A, short-chain ADH, short-chain dehydrogenase/reductase, short-chain NAD(H)-dependent dehydrogenase/reductase, slr1192, SSADH, SsADH-10, SSO2536, ST0053, Ta1316 ADH, TaDH, TBADH, Teth39_0206, Teth39_0218, Teth514_0627, TK0845, Tsac_0416, Y-ADH, YADH, YADH-1, yeast alcohol dehydrogenase, YIM1, YLL056C, YMR152W, Ymr152wp
ECTree
Natural Substrates Products
Natural Substrates Products on EC 1.1.1.1 - alcohol dehydrogenase
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1-butanol + NAD+
butanal + NADH + H+
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-
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?
2-dehydro-3-deoxy-D-gluconate + NADH + H+
4-deoxy-L-erythro-5-hexoseulose + NAD+
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r
4-deoxy-L-erythro-5-hexoseulose + NAD+
2-dehydro-3-deoxy-D-gluconate + NADH + H+
preferred reaction
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r
a primary alcohol + NAD+
an aldehyde + NADH + H+
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ADH3 is involved in multiple cellular pathways, as diverse as formaldehyde detoxification, retinoid metabolism and NO homeostasis, ADH3 is considered to play only a minor role in hepatic alcohol metabolism because ethanol concentrations rarely exceed 50 mM
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?
acetaldehyde + NADH + H+
ethanol + NAD+
all-trans-retinol + NAD+
all-trans-retinal + NADH
allyl alcohol + NAD+
acrolein + NADH
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-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
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?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
crotyl alcohol + NAD+
crotonaldehyde + NADH
ethanol + NAD+
acetaldehyde + NADH
ethanol + NAD+
acetaldehyde + NADH + H+
isobutyramide + NAD+
?
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r
methylglyoxal + NADH + H+
acetol + NAD+
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r
octanol + NAD+
octanal + NADH
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?
phenylethanol + NAD+
phenylacetaldehyde + NADH + H+
sinapaldehyde + NADH
sinapyl alcohol + NAD+
preferred substrates
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r
sinapaldehyde + NADH + H+
sinalcohol + NAD+
additional information
?
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acetaldehyde + NADH + H+
ethanol + NAD+
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r
acetaldehyde + NADH + H+
ethanol + NAD+
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r
acetaldehyde + NADH + H+
ethanol + NAD+
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r
acetaldehyde + NADH + H+
ethanol + NAD+
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r
acetaldehyde + NADH + H+
ethanol + NAD+
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r
acetaldehyde + NADH + H+
ethanol + NAD+
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?
acetaldehyde + NADH + H+
ethanol + NAD+
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cells with an extra copy of ADH1 display chronological life-span extension. Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1 copy show extended replicative life span and increased Sir2p activity
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?
all-trans-retinol + NAD+
all-trans-retinal + NADH
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ADH4 might be involved in biosynthesis of retinoic acid
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r
all-trans-retinol + NAD+
all-trans-retinal + NADH
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?
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
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r
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
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r
crotyl alcohol + NAD+
crotonaldehyde + NADH
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product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
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?
crotyl alcohol + NAD+
crotonaldehyde + NADH
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product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
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?
ethanol + NAD+
acetaldehyde + NADH
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plays an important role in the metabolism of ethanol
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ethanol + NAD+
acetaldehyde + NADH
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?
ethanol + NAD+
acetaldehyde + NADH
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chi-ADH plays an important role in the metabolism of long chain alcohols and aldehydes
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ethanol + NAD+
acetaldehyde + NADH
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the anodic enzyme form may contribute significantly to alcohol elimination in man, particularly at high concentrations when the other enzyme species are saturated
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?
ethanol + NAD+
acetaldehyde + NADH
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the enzyme plays a significant role in first-pass metabolism of ethanol in human
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?
ethanol + NAD+
acetaldehyde + NADH
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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
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?
ethanol + NAD+
acetaldehyde + NADH
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role of the major liver isoenzyme A2 in ethanol metabolism
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?
ethanol + NAD+
acetaldehyde + NADH
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DH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
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?
ethanol + NAD+
acetaldehyde + NADH
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r
ethanol + NAD+
acetaldehyde + NADH
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rate-limiting step of the alcoholic fermentation
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?
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
ethanol + NAD+
acetaldehyde + NADH + H+
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r
phenylethanol + NAD+
phenylacetaldehyde + NADH + H+
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r
phenylethanol + NAD+
phenylacetaldehyde + NADH + H+
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r
sinapaldehyde + NADH + H+
sinalcohol + NAD+
preferred substrates
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r
sinapaldehyde + NADH + H+
sinalcohol + NAD+
preferred substrates
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r
additional information
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one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
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?
additional information
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one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
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?
additional information
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
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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
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?
additional information
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
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the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate
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additional information
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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
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additional information
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alcohol dehydrogenase activity may not limit alcohol supply for ester production during ripening
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?
additional information
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involvement in the development of male hamster reproductive system
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?
additional information
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enzyme may be involved in the metabolism of dietary wax esters in salmonid fish
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?
additional information
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constitutive enzyme
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additional information
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the enzyme oxidizes alcohols to aldehydes or ketones both for detoxification and metabolic purposes
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additional information
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the physiological direction of the catalytic reaction is reduction rather than oxidation
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additional information
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the physiological direction of the catalytic reaction is reduction rather than oxidation
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additional information
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the physiological direction of the catalytic reaction is reduction rather than oxidation
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additional information
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the physiological direction of the catalytic reaction is reduction rather than oxidation
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additional information
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the physiological direction of the catalytic reaction is reduction rather than oxidation
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additional information
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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
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?
additional information
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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
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?
additional information
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key enzyme in ethanol production
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?