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 |
BRENDA | 1.1.5.5 |
EC2PDB | 1.1.5.5 |
ExplorEnz | 1.1.5.5 |
PRIAM enzyme-specific profiles | 1.1.5.5 |
KEGG Ligand Database for Enzyme Nomenclature | 1.1.5.5 |
IUBMB Enzyme Nomenclature | 1.1.5.5 |
IntEnz | 1.1.5.5 |
MEDLINE | Find literature relating to 1.1.5.5 |
MetaCyc | 1.1.5.5 |
Rhea expert-curated reactions | 1.1.5.5 |
UniProtKB/Swiss-Prot |
|
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