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Information on EC 1.1.5.5 - alcohol dehydrogenase (quinone)

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IUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
membrane-bound alcohol dehydrogenase, pqq-adh, quinoprotein ethanol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein methanol dehydrogenase, quinohemoprotein alcohol dehydrogenase, qh-adh, adh-iig, adh-iib, ppg-dh, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ethanol + ubiquinone = acetaldehyde + ubiquinol
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