Hlorid peroksidaza
Hlorid peroksidaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.11.1.10 | ||||||||
CAS broj | 9055-20-3 | ||||||||
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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Hlorid peroksidaza (EC 1.11.1.10, hloroperoksidaza, CPO, vanadiumska haloperoksidaza) je enzim sa sistematskim imenom hlorid:vodonik-peroksid oksidoreduktaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- RH + hlorid + H2O2 RCl + 2 H2O
Ovaj enzim deluje na niz organskih molekula, formirajući stablne C-Cl veze. On takođe oksiduje bromid i jodid. Enzimi ovog tipa su bilo hem-tiolatni proteini, ili sadrže vanadat.
Reference
- ↑ Morris, D.R. and Hager, L.P. (1966). „Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein”. J. Biol. Chem. 241: 1763-1768. PMID 5949836.
- ↑ Hager, L.P., Hollenberg, P.F., Rand-Meir, T., Chiang, R. and Doubek, D.L. (1975). „Chemistry of peroxidase intermediates”. Ann. N.Y. Acad. Sci. 244: 80-93. PMID 1056179.
- ↑ Theiler, R., Cook, J.C., Hager, L.P. and Siuda, J.F. (1978). „Halohydrocarbon synthesis by homoperoxidase”. Science 202: 1094-1096.
- ↑ Sundaramoorthy, M., Terner, J. and Poulos, T.L. (1995). „The crystal structure of chloroperoxidase: a heme peroxidase—cytochrome P450 functional hybrid”. Structure 3: 1367-1377. PMID 8747463.
- ↑ ten Brink, H.B., Tuynman, A., Dekker, H.L., Hemrika, W., Izumi, Y., Oshiro, T., Schoemaker, H.E. and Wever, R. (1998). „Enantioselective sulfoxidation catalyzed by vanadium haloperoxidases”. Inorg. Chem. 37: 6780-6784. PMID 11670813.
- ↑ ten Brink, H.B., Dekker, H.L., Schoemaker, H.E. and Wever, R. (2000). „Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis”. J. Inorg. Biochem. 80: 91-98. PMID 10885468.
- ↑ Manoj, K.M. (2006). „Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process”. Biochim. Biophys. Acta 1764: 1325-1339. PMID 16870515.
- ↑ Kuhnel, K., Blankenfeldt, W., Terner, J. and Schlichting, I. (2006). „Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate”. J. Biol. Chem. 281: 23990-23998. PMID 16790441.
- ↑ Manoj, K.M. and Hager, L.P. (2008). „Chloroperoxidase, a janus enzyme”. Biochemistry 47: 2997-3003. PMID 18220360.
Literatura
- 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.