Alkene monooxygenase
| Alkene monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
Alkene monooxygenase (EC 1.14.13.69) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are propylene, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are propylene oxide, oxidised NAD+, and water.[1][2]
This enzyme is an oxidoreductase, acting on paired donors, with molecular oxygen as oxidant and incorporating one of its atoms. The systematic name of this enzyme class is alkene,NADH:oxygen oxidoreductase. This enzyme is also called alkene epoxygenase. It contains a Rieske type of ferredoxin.[3][4]
Substrate range
The enzyme from a Xanthobacter bacterial species has four peptide components, all of which are required for activity. These oxidise a large range of double bonds, including internal or terminal alkenes and chlorinated derivatives.[5]
When propene is the substrate, the epoxide product is 95% the (R) enantiomer.[6]
References
- ^ Enzyme 1.14.13.69 at KEGG Pathway Database.
- ^ Zhou, Ning-Yi; Jenkins, Alister; Chan Kwo Chion, Chan K. N.; Leak, David J. (1999). "The Alkene Monooxygenase from Xanthobacter Strain Py2 is Closely Related to Aromatic Monooxygenases and Catalyzes Aromatic Monohydroxylation of Benzene, Toluene, and Phenol". Applied and Environmental Microbiology. 65 (4): 1589–1595. doi:10.1128/AEM.65.4.1589-1595.1999. PMC 91225. PMID 10103255.
- ^ Champreda, Verawat; Zhou, Ning-Yi; Leak, David J. (2004). "Heterologous expression of alkene monooxygenase components from Xanthobacter autotrophicus Py2 and reconstitution of the active complex". FEMS Microbiology Letters. 239 (2): 309–318. doi:10.1016/j.femsle.2004.09.002. PMID 15476981.
- ^ Champreda, Verawat; Choi, Young-Jun; Zhou, Ning-Yi; Leak, David J. (2006). "Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions". Applied Microbiology and Biotechnology. 71 (6): 840–847. doi:10.1007/s00253-005-0208-2. PMID 16402171.
- ^ Small, Frederick J.; Ensign, Scott A. (1997). "Alkene Monooxygenase from Xanthobacter Strain Py2". Journal of Biological Chemistry. 272 (40): 24913–24920. doi:10.1074/jbc.272.40.24913. PMID 9312093.
- ^ Gallagher, Stephen C.; Cammack, Richard; Dalton, Howard (1997). "Alkene Monooxygenase from Nocardia Corallina B-276 is a Member of the Class of Dinuclear Iron Proteins Capable of Stereospecific Epoxygenation Reactions". European Journal of Biochemistry. 247 (2): 635–641. doi:10.1111/j.1432-1033.1997.00635.x. PMID 9266707.