(2,2,3-Trimetil-5-oksociklopent-3-enil)acetil-KoA 1,5-monooksigenaza
(2,2,3-Trimetil-5-oksociklopent-3-enil)acetil-KoA 1,5-monooksigenaza (EC 1.14.13.160, 2-okso-Delta3-4,5,5-trimetilciklopentenilacetil-KoA monooksigenaza, 2-okso-Delta3-4,5,5-trimetilciklopentenilacetil-KoA 1,2-monooksigenaza, OTEMO) je enzim sa sistematskim imenom ((1R)-2,2,3-trimetil-5-oksociklopent-3-enil)acetil-KoA,NADPH:kiseonik oksidoreduktaza (1,5-laktonizacija).[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
| (2,2,3-Trimetil-5-oksociklopent-3-enil)acetil-KoA 1,5-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.160 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- [(1R)-2,2,3-trimetil-5-oksociklopent-3-enil]acetil-KoA + O2 + NADPH + H+ [(2R)-3,3,4-trimetil-6-okso-3,6-dihidro-1H-piran-2-il]acetil-KoA + NADP+ + H2O
Ovaj FAD zavisni enzim je izolovan iz Pseudomonas putida.
Reference уреди
- ^ Ougham, H.J., Taylor, D.G. and Trudgill, P.W. (1983). „Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida”. J. Bacteriol. 153: 140—152. PMID 6848481.
- ^ Leisch, H., Shi, R., Grosse, S., Morley, K., Bergeron, H., Cygler, M., Iwaki, H., Hasegawa, Y. and Lau, P.C. (2012). „Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453”. Appl. Environ. Microbiol. 78: 2200—2212. PMID 22267661.
- ^ Kadow, M., Loschinski, K., Sass, S., Schmidt, M. and Bornscheuer, U.T. (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”. Appl. Microbiol. Biotechnol.: —. PMID 22286514.
Literatura уреди
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze уреди
- (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA+1,5-monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)
