EC 1.14.18.3 - Methane monooxygenase (particulate)

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IntEnz Enzyme Nomenclature
EC 1.14.18.3

Names

Accepted name:
methane monooxygenase (particulate)
Systematic name:
methane,quinol:oxygen oxidoreductase

Reaction

Cofactor

Comments:

Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Shiemke, A. K., Cook, S. A., Miley, T., Singleton, P.
    Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors.
    Arch. Biochem. Biophys. 321: 421-428 (1995). [PMID: 7646068]
  2. Basu, P., Katterle, B., Andersson, K. K., Dalton, H.
    The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein.
    Biochem. J. 369: 417-427 (2003). [PMID: 12379148]
  3. Kitmitto, A., Myronova, N., Basu, P., Dalton, H.
    Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath).
    Biochemistry 44: 10954-10965 (2005). [PMID: 16101279]
  4. Balasubramanian, R., Rosenzweig, A. C.
    Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase.
    Acc. Chem. Res. 40: 573-580 (2007). [PMID: 17444606]

[EC 1.14.18.3 created 2011]