Alcohol dehydrogenase (EC 1.1.1.1) (ADH) catalyzes the reversible oxidation of
ethanol to acetaldehyde with the concomitant reduction of NAD [1]. 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) [2], as well as in
Zymomonas mobilis (gene adhB) [3]. These two iron-containing ADH's are closely
related to the following enzymes:
Escherichia coli propanediol oxidoreductase (EC 1.1.1.77) (gene fucO) [4],
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) [5], an enzyme which has activity
using butanol and ethanol as substrates.
Escherichia coli adhE [6], an iron-dependent enzyme which harbor three
different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase
(acetylating) (EC 1.2.1.10) and pyruvate-formate-lyase deactivase.
Bacterial glycerol dehydrogenase (EC 1.1.1.6) (gene gldA or dhaD) [7].
Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae.
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