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Information on EC - alcohol dehydrogenase (quinone)

for references in articles please use BRENDA:EC1.1.5.5

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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, oxidising a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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

ethanol + ubiquinone = acetaldehyde + ubiquinol
show the reaction diagram