EC 1.1.2.7 - Methanol dehydrogenase (cytochrome c)

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IntEnz Enzyme Nomenclature
EC 1.1.2.7

Names

Accepted name:
methanol dehydrogenase (cytochrome c)
Other names:
methanol dehydrogenase
MDH
Systematic name:
methanol:cytochrome c oxidoreductase

Reactions

Cofactor

Comments:

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 methosulphate. 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 disulphide 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).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052932 , GO:0052933 , GO:0052931 , GO:0052930
UniProtKB/Swiss-Prot:

References

  1. Anthony, C., Zatman, L. J.
    The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27.
    Biochem. J. 92: 614-621 (1964). [PMID: 4378696]
  2. Anthony, C., Zatman, L. J.
    The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group.
    Biochem. J. 104: 960-969 (1967). [PMID: 6049934]
  3. Duine, J. A., Frank, J., Verwiel, P. E.
    Structure and activity of the prosthetic group of methanol dehydrogenase.
    Eur. J. Biochem. 108: 187-192 (1980). [PMID: 6250827]
  4. Salisbury, S. A., Forrest, H. S., Cruse, W. B., Kennard, O.
    A novel coenzyme from bacterial primary alcohol dehydrogenases.
    Nature 280: 843-844 (1979). [PMID: 471057]
  5. Cox, J. M., Day, D. J., Anthony, C.
    The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria.
    Biochim. Biophys. Acta 1119: 97-106 (1992). [PMID: 1311606]
  6. Blake, C. C., Ghosh, M., Harlos, K., Avezoux, A., Anthony, C.
    The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues.
    Nat. Struct. Biol. 1: 102-105 (1994). [PMID: 7656012]
  7. Xia, Z. X., He, Y. N., Dai, W. W., White, S. A., Boyd, G. D., Mathews, F. S.
    Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution.
    Biochemistry 38: 1214-1220 (1999). [PMID: 9930981]
  8. Afolabi, P. R., Mohammed, F., Amaratunga, K., Majekodunmi, O., Dales, S. L., Gill, R., Thompson, D., Cooper, J. B., Wood, S. P., Goodwin, P. M., Anthony, C.
    Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL.
    Biochemistry 40: 9799-9809 (2001). [PMID: 11502173]
  9. Anthony, C., Williams, P.
    The structure and mechanism of methanol dehydrogenase.
    Biochim. Biophys. Acta 1647: 18-23 (2003). [PMID: 12686102]
  10. Williams, P. A., Coates, L., Mohammed, F., Gill, R., Erskine, P. T., Coker, A., Wood, S. P., Anthony, C., Cooper, J. B.
    The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens.
    Acta Crystallogr. D Biol. Crystallogr. 61: 75-79 (2005). [PMID: 15608378]

[EC 1.1.2.7 created 1972 as 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.7]