Methane monooxygenase (particulate)
| Methane monooxygenase (particulate) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.18.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Methane monooxygenase (particulate) (EC 1.14.18.3) is an enzyme with systematic name methane,quinol:oxygen oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
Methane monooxygenase contains copper. It is membrane-bound.
References
- ↑ Shiemke, A.K.; Cook, S.A.; Miley, T.; Singleton, P. (1995). "Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors". Arch. Biochem. Biophys. 321 (2): 421–428. doi:10.1006/abbi.1995.1413. PMID 7646068.
- ↑ Basu, P.; Katterle, B.; Andersson, K.K.; Dalton, H. (2003). "The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein". Biochem. J. 369 (Pt 2): 417–427. doi:10.1042/BJ20020823. PMC 1223091
. PMID 12379148. - ↑ Kitmitto, A.; Myronova, N.; Basu, P.; Dalton, H. (2005). "Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)". Biochemistry. 44 (33): 10954–10965. doi:10.1021/bi050820u. PMID 16101279.
- ↑ Balasubramanian, R.; Rosenzweig, A.C. (2007). "Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase". Acc. Chem. Res. 40 (7): 573–580. doi:10.1021/ar700004s. PMID 17444606.
See also
External links
- Methane monooxygenase (particulate) at the US National Library of Medicine Medical Subject Headings (MeSH)
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