ENZYME entry: EC 1.1.2.8
| Accepted Name |
| Alcohol dehydrogenase (cytochrome c).
|
| Reaction catalysed |
| A primary alcohol + 2 cytochrome c <=> an aldehyde + 2 reduced cytochrome c + 2 H(+) |
| Cofactor(s) |
| Pyrroloquinoline quinone.
|
| Comment(s) |
- A periplasmic PQQ-containing quinoprotein.
- Occurs in Pseudomonas and Rhodopseudomonas.
- The enzyme from Pseudomonas aeruginosa uses a specific inducible
cytochrome c(550) as electron acceptor.
- Acts on a wide range of primary and secondary alcohols, but not
methanol.
- It has a homodimeric structure (contrasting with the heterotetrameric
structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)).
- It is routinely assayed with phenazine methosulfate as electron
acceptor.
- Activity is stimulated by ammonia or amines.
- Like all other quinoprotein alcohol dehydrogenases it 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.
- Formerly EC 1.1.99.8.
|
| Cross-references |
| BRENDA | 1.1.2.8 |
| EC2PDB | 1.1.2.8 |
| ExplorEnz | 1.1.2.8 |
| PRIAM enzyme-specific profiles | 1.1.2.8 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.2.8 |
| IUBMB Enzyme Nomenclature | 1.1.2.8 |
| IntEnz | 1.1.2.8 |
| MEDLINE | Find literature relating to 1.1.2.8 |
| MetaCyc | 1.1.2.8 |
| UniProtKB/Swiss-Prot |
|
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