ENZYME entry: EC 18.104.22.168
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|alcohol dehydrogenase (quinone).
|PQQ alcohol dehydrogenase.|
|PQQ-dependent alcohol dehydrogenase.|
|pyrroloquinoline quinone-dependent alcohol dehydrogenase.|
|quinoprotein alcohol dehydrogenase.|
|type III ADH.|
|a ubiquinone + ethanol <=> a ubiquinol + acetaldehyde|
- Only described in acetic acid bacteria where it is involved in acetic
- 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
- It is assayed with phenazine methosulfate or with ferricyanide.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
entries corresponding to 1.1.5.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-