Alcohol dehydrogenase (EC 188.8.131.52) (ADH) catalyzes the reversible oxidation of
ethanol to acetaldehyde with the concomitant reduction of NAD . Currently
three, structurally and catalytically, different types of alcohol
dehydrogenases are known:
Insect-type, or 'short-chain' alcohol dehydrogenases.
Iron-containing alcohol dehydrogenases.
Iron-containing ADH's have been found in yeast (gene ADH4) , as well as in
Zymomonas mobilis (gene adhB) . These two iron-containing ADH's are closely
related to the following enzymes:
Escherichia coli propanediol oxidoreductase (EC 184.108.40.206) (gene fucO) ,
an enzyme involved in the metabolism of fucose and which also seems to
contain ferrous ion(s).
Clostridium acetobutylicum NADPH- and NADH-dependent butanol dehydrogenases
(EC 1.1.1.-) (genes adh1, bdhA and bdhB) , an enzyme which has activity
using butanol and ethanol as substrates.
Escherichia coli adhE , an iron-dependent enzyme which harbor three
different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase
(acetylating) (EC 220.127.116.11) and pyruvate-formate-lyase deactivase.
Bacterial glycerol dehydrogenase (EC 18.104.22.168) (gene gldA or dhaD) .
de Vries G.E., Arfman N., Terpstra P., Dijkhuizen L.
J. Bacteriol. 174:5346-5353(1992).
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