The Enzyme Database

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Accepted name: methanol dehydrogenase (cytochrome c)
Reaction: a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
Other name(s): methanol dehydrogenase; MDH (ambiguous)
Systematic name: methanol:cytochrome c oxidoreductase
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 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, 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: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37205-43-9
1.  Anthony, C. and Zatman, L.J. The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27. Biochem. J. 92 (1964) 614–621. [PMID: 4378696]
2.  Anthony, C. and 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 (1967) 960–969. [PMID: 6049934]
3.  Duine, J.A., Frank, J. and Verweil, P.E.J. Structure and activity of the prosthetic group of methanol dehydrogenase. Eur. J. Biochem. 108 (1980) 187–192. [DOI] [PMID: 6250827]
4.  Salisbury, S.A., Forrest, H.S., Cruse, W.B.T. and Kennard, O. A novel coenzyme from bacterial primary alcohol dehydrogenases. Nature (Lond.) 280 (1979) 843–844. [PMID: 471057]
5.  Cox, J.M., Day, D.J. and Anthony, C. The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria. Biochim. Biophys. Acta 1119 (1992) 97–106. [DOI] [PMID: 1311606]
6.  Blake, C.C., Ghosh, M., Harlos, K., Avezoux, A. and Anthony, C. The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues. Nat. Struct. Biol. 1 (1994) 102–105. [PMID: 7656012]
7.  Xia, Z.X., He, Y.N., Dai, W.W., White, S.A., Boyd, G.D. and 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 (1999) 1214–1220. [DOI] [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. and Anthony, C. Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL. Biochemistry 40 (2001) 9799–9809. [DOI] [PMID: 11502173]
9.  Anthony, C. and Williams, P. The structure and mechanism of methanol dehydrogenase. Biochim. Biophys. Acta 1647 (2003) 18–23. [DOI] [PMID: 12686102]
10.  Williams, P.A., Coates, L., Mohammed, F., Gill, R., Erskine, P.T., Coker, A., Wood, S.P., Anthony, C. and Cooper, J.B. The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 75–79. [DOI] [PMID: 15608378]
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