Kamfor 1,2-monooksigenaza
(Preusmjereno sa stranice (+)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,2-lactonizing))
Kamfor 1,2-monooksigenaza (EC 1.14.15.2, 2,5-diketokamfan laktonizirajući enzim, kamforna ketolaktonaza I, ketolaktonaza I) je enzim sa sistematskim imenom (+)-kamfor,redukovani-rubredoksin:kiseonik oksidoreduktaza (1,2-laktonizacija).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju:
| Kamfor 1,2-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.15.2 | ||||||||
| CAS broj | 37256-81-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (+)-bornan-2,5-dion + redukovani rubredoksin + O2 5-okso-1,2-kamfolid + oksidovani rubredoksin + H2O
Ovaj enzim je flavoprotein za čije dejstvo je neophodno Fe2+. On je izolovan iz Pseudomonas putida. Produkt se spontano konvertuje u [(1R)-5-okso-2,2,3-trimetilciklopent-3-enil]acetat.
Reference uredi
- ↑ Conrad, H.E., DuBus, R., Namtvedt, M.J. and Gunsalus, I.C. (1965). „Mixed function oxidation. II. Separation and properties of the enzymes catalyzing camphor lactonizaton”. J. Biol. Chem. 240: 495-503. PMID 14253460.
- ↑ Trudgill, P.W., DuBus, R. and Gunsalus, I.C. (1966). „Mixed function oxidation. VI. Purification of a tightly coupled electron transport complex in camphor lactonization”. J. Biol. Chem. 241: 4288-4290. PMID 4288652.
- ↑ Yu, C.A. and Gunsalus, I.C. (1969). „Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components”. J. Biol. Chem. 244: 6149-6152. PMID 4310834.
- ↑ Taylor, D.G. and Trudgill, P.W. (1986). „Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453”. J. Bacteriol. 165: 489-497. PMID 3944058.
- ↑ Lounnas, V. and Wade, R.C. (1997). „Exceptionally stable salt bridges in cytochrome P450cam have functional roles”. Biochemistry 36: 5402-5417. PMID 9154922.
- ↑ Kadow, M., Sass, S., Schmidt, M. and Bornscheuer, U.T. (2011). „Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007”. AMB Express 1: #13-13. PMID 21906366.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.