Alcohol dehydrogenase (EC 184.108.40.206) (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 220.127.116.11) (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 18.104.22.168) and pyruvate-formate-lyase deactivase.
Bacterial glycerol dehydrogenase (EC 22.214.171.124) (gene gldA or dhaD) .
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see prosite_license.html.