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 broj1.11.2.2
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB 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

  1. ^ Agner, K. (1943). „Myeloperoxidase”. Adv. Enzymol. 3: 137—148. 
  2. ^ Harrison, J.E. & Schultz, J. (1976). „Studies on the chlorinating activity of myeloperoxidase”. J. Biol. Chem. 251: 1371—1374. PMID 176150. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ Klebanoff, S.J. (2005). „Myeloperoxidase: friend and foe”. J. Leukoc. Biol. 77: 598—625. PMID 15689384. 
  6. ^ 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. 
  7. ^ 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

Spoljašnje veze уреди