Biology:Methanol dehydrogenase (cytochrome c)
From HandWiki
| Methanol dehydrogenase (cytochrome c) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methanol dehydrogenase homodimer, Methylacidiphilum fumariolicum | |||||||||
| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] an aldehyde + 2 ferrocytochrome cL + 2 H+
A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.
References
- ↑ "The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27". The Biochemical Journal 92 (3): 614–21. September 1964. doi:10.1042/bj0920614. PMID 4378696.
- ↑ "The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". The Biochemical Journal 104 (3): 960–9. September 1967. doi:10.1042/bj1040960. PMID 6049934.
- ↑ "Structure and activity of the prosthetic group of methanol dehydrogenase". European Journal of Biochemistry 108 (1): 187–92. 1980. doi:10.1111/j.1432-1033.1980.tb04711.x. PMID 6250827.
- ↑ "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature 280 (5725): 843–4. August 1979. doi:10.1038/280843a0. PMID 471057.
- ↑ "The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1119 (1): 97–106. February 1992. doi:10.1016/0167-4838(92)90240-E. PMID 1311606.
- ↑ "The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues". Nature Structural Biology 1 (2): 102–5. February 1994. doi:10.1038/nsb0294-102. PMID 7656012.
- ↑ "Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution". Biochemistry 38 (4): 1214–20. January 1999. doi:10.1021/bi9822574. PMID 9930981.
- ↑ "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)". Biochemistry 40 (33): 9799–809. August 2001. doi:10.1021/bi002932l. PMID 11502173.
- ↑ "The structure and mechanism of methanol dehydrogenase". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1647 (1–2): 18–23. April 2003. doi:10.1016/S1570-9639(03)00042-6. PMID 12686102.
- ↑ "The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens". Acta Crystallographica Section D 61 (Pt 1): 75–9. January 2005. 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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