| Methane monooxygenase (particulate) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
&sq=Qlik&lang=&file=File:1yew.jpg) Particulate methane monooxygenase hexa-heterotrimer, Methylococcus capsulatus | |||||||||
| Identifiers | |||||||||
| EC no. | 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 enzyme present in methanotrophs.
- ^ Shiemke AK, Cook SA, Miley T, Singleton P (August 1995). "Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors". Archives of Biochemistry and Biophysics. 321 (2): 421–8. doi:10.1006/abbi.1995.1413. PMID 7646068.
- ^ Basu P, Katterle B, Andersson KK, Dalton H (January 2003). "The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein". The Biochemical Journal. 369 (Pt 2): 417–27. doi:10.1042/BJ20020823. PMC 1223091. PMID 12379148.
- ^ Kitmitto A, Myronova N, Basu P, Dalton H (August 2005). "Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)". Biochemistry. 44 (33): 10954–65. doi:10.1021/bi050820u. PMID 16101279.
- ^ Balasubramanian R, Rosenzweig AC (July 2007). "Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase". Accounts of Chemical Research. 40 (7): 573–80. doi:10.1021/ar700004s. PMID 17444606.