Methanol dehydrogenase (cytochrome c)

Methanol dehydrogenase (cytochrome c)
Identifiers
EC number 1.1.2.7
CAS number 37205-43-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Methanol dehydrogenase (cytochrome c) (EC 1.1.2.7, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase.[1][2][3][4][5][6][7][8][9][10] This enzyme catalyses the following chemical reaction

a primary alcohol + 2 ferricytochrome cL \rightleftharpoons an aldehyde + 2 ferrocytochrome cL + 2 H+

A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.

References

  1. ↑ Anthony, C. and Zatman, L.J. (1964). "The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27". Biochem. J. 92 (3): 614–621. PMC 1206111. PMID 4378696.
  2. ↑ Anthony, C. and Zatman, L.J. (1967). "The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". Biochem. J. 104 (3): 960–969. PMC 1271238. PMID 6049934.
  3. ↑ Duine, J.A., Frank, J. and Verweil, P.E.J. (1980). "Structure and activity of the prosthetic group of methanol dehydrogenase". Eur. J. Biochem. 108 (1): 187–192. doi:10.1111/j.1432-1033.1980.tb04711.x. PMID 6250827.
  4. ↑ Salisbury, S.A., Forrest, H.S., Cruse, W.B.T. and Kennard, O. (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature (Lond.) 280 (5725): 843–844. doi:10.1038/280843a0. PMID 471057.
  5. ↑ Cox, J.M., Day, D.J. and Anthony, C. (1992). "The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria". Biochim. Biophys. Acta 1119: 97–106. doi:10.1016/0167-4838(92)90240-E. PMID 1311606.
  6. ↑ Blake, C.C., Ghosh, M., Harlos, K., Avezoux, A. and Anthony, C. (1994). "The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues". Nat. Struct. Biol. 1 (2): 102–105. doi:10.1038/nsb0294-102. PMID 7656012.
  7. ↑ Xia, Z.X., He, Y.N., Dai, W.W., White, S.A., Boyd, G.D. and Mathews, F.S. (1999). "Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution". Biochemistry 38 (4): 1214–1220. doi:10.1021/bi9822574. 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. (2001). "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome cL". Biochemistry 40 (33): 9799–9809. doi:10.1021/bi002932l. PMID 11502173.
  9. ↑ Anthony, C. and Williams, P. (2003). "The structure and mechanism of methanol dehydrogenase". Biochim. Biophys. Acta 1647: 18–23. doi:10.1016/S1570-9639(03)00042-6. 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. (2005). "The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens". Acta Crystallogr. D Biol. Crystallogr. 61 (Pt 1): 75–79. doi:10.1107/S0907444904026964. PMID 15608378.

External links

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