Alkene monooxygenase
Appearance
alkene monooxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.13.69 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an alkene monooxygenase (EC 1.14.13.69) is an enzyme that catalyzes the chemical reaction
- propene + NADH + H+ + O2 1,2-epoxypropane + NAD+ + H2O
The 4 substrates of this enzyme are propene, NADH, H+, and O2, whereas its 3 products are 1,2-epoxypropane, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is alkene,NADH:oxygen oxidoreductase. This enzyme is also called alkene epoxygenase. This enzyme participates in tetrachloroethene degradation.
References
[edit]- Small FJ, Ensign SA (1997). "Alkene monooxygenase from Xanthobacter strain Py2. Purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes". J. Biol. Chem. 272 (40): 24913–20. doi:10.1074/jbc.272.40.24913. PMID 9312093.
- Zhou NY, Jenkins A, Chan Kwo Chion CK, Leak DJ (1999). "The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol". Appl. Environ. Microbiol. 65 (4): 1589–95. PMC 91225. PMID 10103255.
- Gallagher SC, Cammack R, Dalton H (1997). "Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions". Eur. J. Biochem. 247 (2): 635–41. doi:10.1111/j.1432-1033.1997.00635.x. PMID 9266707.