ENZYME entry: EC 220.127.116.11
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|methanol dehydrogenase (cytochrome c).
|a primary alcohol + 2 Fe(III)-[cytochrome cL] <=> an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+)|
- A periplasmic quinoprotein alcohol dehydrogenase that only occurs in
- It uses the novel specific cytochrome cL as acceptor.
- Acts on a wide range of primary alcohols, including ethanol,
duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde.
- Activity is stimulated by ammonia or methylamine.
- It is usually assayed with phenazine methosulfate.
- 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
- It differs from EC 18.104.22.168, alcohol dehydrogenase (cytochrome c),
in having a high affinity for methanol and in having a second
essential small subunit (no known function).
- Formerly EC 22.214.171.124.
|PRIAM enzyme-specific profiles||126.96.36.199|
|KEGG Ligand Database for Enzyme Nomenclature||188.8.131.52|
|IUBMB Enzyme Nomenclature||184.108.40.206|
|MEDLINE||Find literature relating to 220.127.116.11|
|Rhea expert-curated reactions||18.104.22.168|
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.-.-.-