1.11.2.2: myeloperoxidase
This is an abbreviated version!
For detailed information about myeloperoxidase, go to the full flat file.
Word Map on EC 1.11.2.2
-
1.11.2.2
-
neutrophil
-
necrosis
-
leukocyte
-
tnf
-
malondialdehyde
-
dismutase
-
colitis
-
reperfusion
-
pulmonary
-
artery
-
endothelial
-
polymorphonuclear
-
ischemia
-
catalase
-
monocyte
-
sham
-
bowel
-
lps
-
mucosal
-
ulcer
-
edema
-
bronchoalveolar
-
wistar
-
granulocyte
-
lavage
-
lipopolysaccharide
-
sod
-
hypochlorous
-
hocl
-
vasculitis
-
ischemia-reperfusion
-
factor-alpha
-
macroscopic
-
tnf-alpha
-
eosinophil
-
elastase
-
dextran
-
ancas
-
myeloid
-
dss-induced
-
degranulation
-
glomerulonephritis
-
lactoferrin
-
icam-1
-
granulomatosis
-
antineutrophil
-
instil
-
medicine
-
carrageenan-induced
-
lactoperoxidase
-
crescent
-
analysis
- 1.11.2.2
- neutrophil
- necrosis
- leukocyte
- tnf
- malondialdehyde
- dismutase
- colitis
-
reperfusion
- pulmonary
- artery
- endothelial
-
polymorphonuclear
- ischemia
- catalase
- monocyte
-
sham
- bowel
- lps
- mucosal
- ulcer
- edema
-
bronchoalveolar
- wistar
- granulocyte
-
lavage
- lipopolysaccharide
- sod
-
hypochlorous
- hocl
- vasculitis
-
ischemia-reperfusion
- factor-alpha
-
macroscopic
- tnf-alpha
-
eosinophil
- elastase
- dextran
-
ancas
- myeloid
-
dss-induced
-
degranulation
- glomerulonephritis
- lactoferrin
- icam-1
- granulomatosis
-
antineutrophil
-
instil
- medicine
-
carrageenan-induced
- lactoperoxidase
-
crescent
- analysis
Reaction
Synonyms
donor, hydrogen peroxide oxidoreductase, donor, hydrogen peroxideoxidoreductase, donor: H2O2 oxidoreductase, donor:H2O2 oxidoreductase, donor:hydrogen peroxide oxidoreductase, donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7, epx2a, hemi-MPO, hemi-myeloperoxidase, LPO, MPO, MPX, myeloperoxidase, peroxinectin, properoxinectin, recombinant human MPO, rhMPO, tissue myeloperoxidase
ECTree
Advanced search results
General Information
General Information on EC 1.11.2.2 - myeloperoxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
malfunction
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
physiological function
-
mice deficient in myeloperoxidase are more likely than wild type mice to die from infection by polymicrobial sepsis
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
malfunction
genetic deficiency in enzyme is associated with chronic and persistent infections, particularly by the fungus Candida albicans
-
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
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
physiological function
-
HOCl generated by the MPO-H2O2-chloride system inactivates tissue inhibitor of metalloproteinase-1 by oxidizing its N-terminal cysteine
physiological function
-
human neutrophils use the myeloperoxidase-hydrogen peroxide-chloride system to chlorinate but not nitrate Escherichia coli proteins during phagocytosis
physiological function
-
hypochlorite formed by the MPO-H2O2-Cl- system is responsible for modification in unsaturated phosphatidylcholines (e.g. 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, 1-palmitoyl-2arachidonoyl-sn-glycero-3-phosphocholine, 1-stearoyl-2-linoleoyl-sn-glycero-3-phosphocholine, or 1-palmitoyl-2-docosahexenoyl-sn-glycero-3-phosphocholine). The formation of lysophospholipids and chlorohydrins from unsaturated phosphatidylcholines by myeloperoxidase can be relevant in vivo under acute inflammatory conditions
physiological function
-
MPO is involved in the defence mechanism of the body against microorganisms
physiological function
myeloperoxidase plays a fundamental role in oxidant production by neutrophils
physiological function
-
myeloperoxidase protects against sepsis in vivo by producing halogenating species, myeloperoxidase plays an important role in host defense against bacterial pathogens
physiological function
oxidation of serotonin by myeloperoxidase may profoundly influence inflammatory processes
physiological function
-
upon the action of the MPO-H2O2-chloride system, two of the major functional activities of kininogens: the susceptibility of high-molecular mass kininogen and low-molecular mass kininogen to kinin-forming action of kallikreins and the prekallikrein-binding capability of high-molecular mass kininogen, are dramatically impaired
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
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
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
physiological function
myeloperoxidase is a key player in oxidative killing of bacteria. This enzyme uses superoxide and hydrogen peroxide to generate hypochlorous acid - a strong oxidant that is toxic to all bacteria
physiological function
stimulation of endothelial-transcytosed enzyme activates endothelial nitric oxide synthase (eNOS) by promoting phospholipase C-dependent calcium signaling and altered eNOS phosphorylation at Ser-1179 and Thr-497. This may constitute a compensatory signaling response of endothelial cells aimed at maintaining eNOS activity and nitric oxide production in the face of enzyme-catalyzed oxidative stress
physiological function
the enzyme has a protective role in bone turnover by limiting osteoclastogenesis and bone resorption physiologically through modulating intracellular H2O2 level. Enzyme overexpression suppressed reactive oxygen species production in mouse osteoclast precursors
physiological function
the enzyme has no effect on the low procoagulant activity of silica-free DNA
physiological function
the monomeric as well as the dimeric enzyme form bind to the glycophorins A/B and band 3 protein on red blood cell's plasma membrane, that lead to reduced cell resistance to osmotic and acidic hemolysis, reduction in cell elasticity, significant changes in cell volume, morphology, and the conductance of red blood cell plasma membrane ion channels. Furthermore, both dimeric and monomeric enzyme forms lead to phosphatidylserine exposure on the outer leaflet of red blood cell membrane