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1.1.1.1: alcohol dehydrogenase

This is an abbreviated version!
For detailed information about alcohol dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.1

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

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase

Subunits

Subunits on EC 1.1.1.1 - alcohol dehydrogenase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
Megalodesulfovibrio gigas
-
10 * 43000, SDS-PAGE
dodecamer
12 * 35000, SDS-PAGE
homodimer
homotetramer
monomer
octamer
oligomer
the enzyme occurs in an oligomeric form called spirosomes. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. CryoEM analysis of the AdhE spirosomes in their compact and extended forms, enzyme filaments and quarternary structure analysis, overview
tetramer
trimer
additional information