Mijeloperoksidaza
| Mijeloperoksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.11.2.2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Mijeloperoksidaza (EC 1.11.2.2, MPO, verdoperoksidaza) je enzim sa sistematskim imenom hlorid:vodonik-peroksid oksidoreduktaza (formira hipohlorit).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Cl- + H2O2 + H+ HClO + H2O
Ovaj enzim sadrži kalcijum i kovalentno vezani hem. On je presutan u fagozomima neutrofila i monocita, gde je formirani hipohlorit veoma baktericidan.
Reference
- ↑ Agner, K. (1943). „Myeloperoxidase”. Adv. Enzymol. 3: 137-148.
- ↑ Harrison, J.E. and Schultz, J. (1976). „Studies on the chlorinating activity of myeloperoxidase”. J. Biol. Chem. 251: 1371-1374. PMID 176150.
- ↑ Furtmuller, P.G., Burner, U. and Obinger, C. (1998). „Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate”. Biochemistry 37: 17923-17930. PMID 9922160.
- ↑ Tuynman, A., Spelberg, J.L., Kooter, I.M., Schoemaker, H.E. and Wever, R. (2000). „Enantioselective epoxidation and carbon-carbon bond cleavage catalyzed by Coprinus cinereus peroxidase and myeloperoxidase”. J. Biol. Chem. 275: 3025-3030. PMID 10652281.
- ↑ Klebanoff, S.J. (2005). „Myeloperoxidase: friend and foe”. J. Leukoc. Biol. 77: 598-625. PMID 15689384.
- ↑ Fiedler, T.J., Davey, C.A. and Fenna, R.E. (2000). „X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution”. J. Biol. Chem. 275: 11964-11971. PMID 10766826.
- ↑ Gaut, J.P., Yeh, G.C., Tran, H.D., Byun, J., Henderson, J.P., Richter, G.M., Brennan, M.L., Lusis, A.J., Belaaouaj, A., Hotchkiss, R.S. and Heinecke, J.W. (2001). „Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis”. Proc. Natl. Acad. Sci. USA 98: 11961-11966. PMID 11593004.
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.
Spoljašnje veze
- MeSH Myeloperoxidase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
