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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 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
BRENDA1.1.2.7
EC2PDB1.1.2.7
ExplorEnz1.1.2.7
PRIAM enzyme-specific profiles1.1.2.7
KEGG Ligand Database for Enzyme Nomenclature1.1.2.7
IUBMB Enzyme Nomenclature1.1.2.7
IntEnz1.1.2.7
MEDLINEFind literature relating to 1.1.2.7
MetaCyc1.1.2.7
UniProtKB/Swiss-Prot
P16027, DHM1_METEA;  P38539, DHM1_METME;  P15279, DHM1_METOR;  
P12293, DHM1_PARDE;  P14775, DHM2_METEA;  P38540, DHM2_METME;  
Q09053, DHM2_METSP;  P29898, DHM2_PARDE;  

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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.-.-.-