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 an aldehyde + 2 ferrocytochrome cL + 2 H+
A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.
References
- ↑ Anthony, C.; 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. - ↑ Anthony, C.; 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.
- ↑ Duine, J.A.; Frank, J.; 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.
- ↑ Salisbury, S.A.; Forrest, H.S.; Cruse, W.B.T.; Kennard, O. (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature (Lond.). 280 (5725): 843–844. doi:10.1038/280843a0. PMID 471057.
- ↑ Cox, J.M.; Day, D.J.; 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.
- ↑ Blake, C.C.; Ghosh, M.; Harlos, K.; Avezoux, A.; 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.
- ↑ Xia, Z.X.; He, Y.N.; Dai, W.W.; White, S.A.; Boyd, G.D.; 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.
- ↑ 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. (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.
- ↑ Anthony, C.; 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.
- ↑ Williams, P.A.; Coates, L.; Mohammed, F.; Gill, R.; Erskine, P.T.; Coker, A.; Wood, S.P.; Anthony, C.; Cooper, J.B. (2005). "The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens". Acta Crystallogr. D. 61 (Pt 1): 75–79. doi:10.1107/S0907444904026964. PMID 15608378.
External links
- Methanol dehydrogenase (cytochrome c) at the US National Library of Medicine Medical Subject Headings (MeSH)
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