| EC |
1.14.13.25 |
| Accepted name: |
methane monooxygenase (soluble) |
| Reaction: |
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O |
| Other name(s): |
methane hydroxylase |
| Systematic name: |
methane,NAD(P)H:oxygen oxidoreductase (hydroxylating) |
| Comments: |
The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO2, ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51961-97-8 |
| References: |
| 1. |
Colby, J. Stirling, D.I. and Dalton, H. The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds. Biochem. J. 165 (1977) 395–402. [PMID: 411486] |
| 2. |
Hyman, M.R. and Wood, P.M. Methane oxidation by Nitrosomonas europaea. Biochem. J. 212 (1983) 31–37. [PMID: 6870854] |
| 3. |
Stirling, D.I. and Dalton, H. Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). Eur. J. Biochem. 96 (1979) 205–212. [DOI] [PMID: 572296] |
| 4. |
Tonge, G.M., Harrison, D.E.F. and Higgins, I.J. Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b. Biochem. J. 161 (1977) 333–344. [PMID: 15544] |
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| [EC 1.14.13.25 created 1984, modified 2011] |
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