((1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA,NADPH:oxygen oxidoreductase
| (2,2,3-Trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.160 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(2,2,3-Trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase (EC 1.14.13.160, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase, OTEMO) is an enzyme with systematic name ((1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA,NADPH:oxygen oxidoreductase (1,5-lactonizing).[1][2][3] This enzyme catalyses the following chemical reaction
- [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + O2 + NADPH + H+ [(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA + NADP+ + H2O
(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase is FAD dependent enzyme isolated from Pseudomonas putida.
References[]
- ^ Ougham HJ, Taylor DG, Trudgill PW (January 1983). "Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-delta 3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida". Journal of Bacteriology. 153 (1): 140–52. PMC 217351. PMID 6848481.
- ^ Leisch H, Shi R, Grosse S, Morley K, Bergeron H, Cygler M, Iwaki H, Hasegawa Y, Lau PC (April 2012). "Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Δ(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453". Applied and Environmental Microbiology. 78 (7): 2200–12. doi:10.1128/AEM.07694-11. PMC 3302634. PMID 22267661.
- ^ Kadow M, Loschinski K, Sass S, Schmidt M, Bornscheuer UT (October 2012). "Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization". Applied Microbiology and Biotechnology. 96 (2): 419–29. doi:10.1007/s00253-011-3859-1. PMID 22286514.
External links[]
- (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA+1,5-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
