Mijeloperoksidaza
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
| Mijeloperoksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.11.2.2 | ||||||||
| 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 | ||||||||
| |||||||||
- 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
уреди- ^ Agner, K. (1943). „Myeloperoxidase”. Adv. Enzymol. 3: 137—148.
- ^ Harrison, J.E. & 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
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.
Spoljašnje veze
уреди- Myeloperoxidase на US National Library of Medicine Medical Subject Headings (MeSH)
