EC Number   |
General Information |
Reference |
|---|
   1.11.2.2 | malfunction |
genetic ablation of the enzyme results in osteoporotic phenotypes and potentiated bone-resorptive capacity in mice. Mechanistically, accumulation of intracellular H2O2 and reactive oxygen species are observed in enzyme deficiency. The increased reactive oxygen species caused by enzyme deficiency contributes to osteoclastogenesis |
765127 |
| 1.11.2.2 | malfunction |
genetic deficiency in enzyme is associated with chronic and persistent infections, particularly by the fungus Candida albicans |
765515 |
| 1.11.2.2 | malfunction |
mice deficient in myeloperoxidase are more likely than wild type mice to die from infection by polymicrobial sepsis |
713436 |
| 1.11.2.2 | metabolism |
enzyme-mediated damage of lipid-free apolipoprotein A-I impairs its ability to promote cellular cholesterol efflux by the ABCA1 pathway, whereas oxidation to lipid-associated apolipoprotein A-I inhibits lecithin:cholesterol acyltransferase activation, two key steps in reverse cholesterol transport |
764466 |
| 1.11.2.2 | physiological function |
association of the enzyme with high-density lipoprotein leads to lower paraoxonase 1 (PON1) activity in part via isolevuglandin-mediated modification of PON1, so that isolevuglandin modification of PON1 can contribute to increased risk for atherosclerosis |
765080 |
| 1.11.2.2 | physiological function |
at sites of inflammation myeloperoxidase will nitrate proteins, even though nitrite is a poor substrate, because the co-substrate tyrosine will be available to facilitate the reaction |
712342 |
| 1.11.2.2 | physiological function |
balance between peroxidase and chlorinating activities of myeloperoxidase is very important for the enhancement of antimicrobial action and prevention of damage caused by hypochlorite |
711270 |
| 1.11.2.2 | physiological function |
by binding to beta2-integrin (CD11b/CD18), dimeric enzyme induces neutrophil activation and adhesion augmenting leukocyte accumulation at sites of inflammation. Monomeric enzyme is less efficient than dimeric enzyme at inducing actin cytoskeleton reorganization, cell survival, and neutrophil degranulation. The decomposition of dimeric enzyme into monomers can serve as a regulatory mechanism that controls enzyme-dependent activation of neutrophils and reduces the proinflammatory effects of the enzyme. Enzyme-induced increase in cytosolic calcium is due to both Ca2+ release from endoplasmic reticulum and Ca2+ entry from extracellular space through calcium channels in the plasma membrane |
764087 |
| 1.11.2.2 | physiological function |
enzyme binds to the extracellular matrix proteins collagen IV and fibronectin, and this association is enhanced by the pre-incubation of these proteins with glycosaminoglycans. Correspondingly, an excess of glycosaminoglycans in solution during incubation inhibits the binding of enzyme to collagen IV and fibronectin. The oxidizing and chlorinating potential of myeloperoxidase is preserved upon binding to collagen IV and fibronectin, even the potentiation of enzyme activity in the presence of collagen IV and fibronectin is observed |
724461 |
| 1.11.2.2 | physiological function |
HOCl generated by the MPO-H2O2-chloride system inactivates tissue inhibitor of metalloproteinase-1 by oxidizing its N-terminal cysteine |
712361 |
