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ENZYME entry: EC 1.1.5.5

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
Ethanol + ubiquinone <=> acetaldehyde + ubiquinol
Cofactor(s)
Pyrroloquinoline quinone.
Comment(s)
  • 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.
Cross-references
BRENDA1.1.5.5
EC2PDB1.1.5.5
ExplorEnz1.1.5.5
PRIAM enzyme-specific profiles1.1.5.5
KEGG Ligand Database for Enzyme Nomenclature1.1.5.5
IUBMB Enzyme Nomenclature1.1.5.5
IntEnz1.1.5.5
MEDLINEFind literature relating to 1.1.5.5
MetaCyc1.1.5.5
Rhea expert-curated reactions1.1.5.5
UniProtKB/Swiss-Prot
P18278, ADHA_ACEAC;  O05542, ADHA_GLUOX;  P28036, ADHA_GLUPO;  
Q44002, ADHA_KOMEU;  Q47945, ADHB_GLUOX;  P0A388, ADHB_GLUPO;  
P0A389, ADHB_KOMEU;  

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