ENZYME entry: EC 126.96.36.199
View entry in original ENZYME format
View entry in raw text format (no links)
|Alcohol dehydrogenase (quinone).
|PQQ alcohol dehydrogenase.|
|PQQ-dependent alcohol dehydrogenase.|
|Pyrroloquinoline quinone-dependent alcohol dehydrogenase.|
|Quinoprotein alcohol dehydrogenase.|
|Type III ADH.|
|Ethanol + ubiquinone <=> acetaldehyde + ubiquinol|
- 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||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
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.-.-.-