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ENZYME

ENZYME entry: EC 1.1.2.7

PURL: https://purl.expasy.org/enzyme/EC/1.1.2.7
Accepted Name
methanol dehydrogenase (cytochrome c)
Alternative Name(s)
MDH
methanol dehydrogenase
Reaction catalysed
2 Fe(III)-[cytochrome cL] + a primary alcohol = 2 Fe(II)-[cytochrome cL] + an aldehyde + 2 H(+)
Comment(s)
  • A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria.
  • 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 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
KEGG Ligand Database for Enzyme Nomenclature1.1.2.7
IUBMB Enzyme Nomenclature1.1.2.7
MEDLINEFind literature relating to 1.1.2.7
MetaCyc1.1.2.7
Rhea expert-curated reactions1.1.2.7
UniProtKB/Swiss-Prot
P16027, DHM1_METEAP38539, DHM1_METMEP15279, DHM1_METOR
P12293, DHM1_PARDEP14775, DHM2_METEAP38540, DHM2_METME
Q09053, DHM2_METSPP29898, DHM2_PARDE

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