ENZYME entry: EC 1.1.2.7
Accepted Name |
Methanol dehydrogenase (cytochrome c).
|
Alternative Name(s) |
MDH. |
Methanol dehydrogenase. |
Reaction catalysed |
A primary alcohol + 2 cytochrome c(L) <=> an aldehyde + 2 reduced cytochrome c(L) + 2 H(+) |
Cofactor(s) |
Pyrroloquinoline quinone.
|
Comment(s) |
- A periplasmic quinoprotein alcohol dehydrogenase that only occurs in
methylotrophic bacteria.
- It uses the novel specific cytochrome c(L) 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
the PQQ.
- It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c),
in having a high affinity for methanol and in having a second
essential small subunit (no known function).
- Formerly EC 1.1.99.8.
|
Cross-references |
BRENDA | 1.1.2.7 |
EC2PDB | 1.1.2.7 |
ExplorEnz | 1.1.2.7 |
PRIAM enzyme-specific profiles | 1.1.2.7 |
KEGG Ligand Database for Enzyme Nomenclature | 1.1.2.7 |
IUBMB Enzyme Nomenclature | 1.1.2.7 |
IntEnz | 1.1.2.7 |
MEDLINE | Find literature relating to 1.1.2.7 |
MetaCyc | 1.1.2.7 |
Rhea expert-curated reactions | 1.1.2.7 |
UniProtKB/Swiss-Prot |
|
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