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ENZYME entry: EC

Accepted Name
alcohol dehydrogenase (quinone)
Alternative Name(s)
PQQ alcohol dehydrogenase
PQQ-dependent ADH
PQQ-dependent alcohol dehydrogenase
pyrroloquinoline quinone-dependent alcohol dehydrogenase
quinoprotein ADH
quinoprotein alcohol dehydrogenase
type III ADH
Reaction catalysed
a ubiquinone + ethanol <=> a ubiquinol + acetaldehyde
  • 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.
PRIAM enzyme-specific profiles1.1.5.5
KEGG Ligand Database for Enzyme Nomenclature1.1.5.5
IUBMB Enzyme Nomenclature1.1.5.5
MEDLINEFind literature relating to
Rhea expert-curated reactions1.1.5.5

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