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EC 1.1.5.5 Details
show Brenda entryEC number
1.1.5.5
Accepted name
alcohol dehydrogenase (quinone)
Reaction
ethanol + ubiquinone = acetaldehyde + ubiquinol
Other name(s)
type III ADH,
membrane associated quinohaemoprotein alcohol dehydrogenase
Systematic name
alcohol:quinone oxidoreductase
Comment
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
History
created 2009, modified 2010
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1 Oxidoreductases
1.1.1.70 created 1965, deleted 1978 1.1.1.74 created 1972, deleted 1976 1.1.1.89 created 1972, deleted 1976 1.1.1.109 created 1972, deleted 1976 1.1.1.139 created 1972, deleted 1978 1.1.1.155 created 1976, deleted 2004 1.1.1.171 created 1978, deleted 1984 1.1.1.180 created 1983, deleted 1984 1.1.1.182 created 1983, deleted 1990 1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004 1.1.1.242 created 1992, deleted 2001 1.1.1.253 created 1999, deleted 2003
1.1.2 With a cytochrome as acceptor 1.1.5.1 created 1983, deleted 2002
