1,8-Cineol 2-endo-monooksigenaza
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| 1,8-Cineol 2-endo-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.156 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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1,8-Cineol 2-endo-monooksigenaza (EC 1.14.13.156, P450cin, CYP176A, CYP176A1) je enzim sa sistematskim imenom 1,8-cineol,NADPH:kiseonik oksidoreduktaza (2-endo-hidroksilacija).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 1,8-cineol + NADPH + H+ + O2 2-endo-hidroksi-1,8-cineol + NADP+ + H2O
Ovaj enzim je hem-tiolatni protein (P-450) koji koristi flavodoksinu sličnog redoks partnera da redukuje gvožđehema.
Reference[uredi | uredi kod]
- ↑ Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. (2002). „Cytochrome P450cin (CYP176A), isolation, expression, and characterization”. J. Biol. Chem. 277: 27725-27732. PMID 12016226.
- ↑ Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. (2004). „Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam”. Biochemistry 43: 9487-9494. PMID 15260491.
- ↑ Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. (2007). „Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin”. J. Biol. Chem. 282: 27006-27011. PMID 17606612.
- ↑ Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. (2008). „The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin”. J. Biol. Chem. 283: 10804-10812. PMID 18270198.
Literatura[uredi | uredi kod]
- 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.