A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 188.8.131.52
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|Alcohol dehydrogenase (cytochrome c).
|A primary alcohol + 2 cytochrome c <=> an aldehyde + 2 reduced cytochrome c + 2 H(+)|
- 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
- It has a homodimeric structure (contrasting with the heterotetrameric
structure of EC 184.108.40.206, methanol dehydrogenase (cytochrome c)).
- It is routinely assayed with phenazine methosulfate as electron
- 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
- Formerly EC 220.127.116.11.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
entries corresponding to 1.1.2.-
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