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 |
Rhea expert-curated reactions | 1.1.2.8 |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.1.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-