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
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1.11.2.2
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neutrophil
-
necrosis
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leukocyte
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tnf
-
malondialdehyde
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dismutase
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colitis
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reperfusion
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pulmonary
-
artery
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endothelial
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polymorphonuclear
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ischemia
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catalase
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monocyte
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sham
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bowel
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lps
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mucosal
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ulcer
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edema
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bronchoalveolar
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wistar
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granulocyte
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lavage
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lipopolysaccharide
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sod
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hypochlorous
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hocl
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vasculitis
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ischemia-reperfusion
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factor-alpha
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macroscopic
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tnf-alpha
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eosinophil
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elastase
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dextran
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ancas
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myeloid
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dss-induced
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degranulation
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glomerulonephritis
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lactoferrin
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icam-1
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granulomatosis
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antineutrophil
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instil
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medicine
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carrageenan-induced
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lactoperoxidase
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crescent
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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
1.11.2.2 myeloperoxidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.11.2.2 - myeloperoxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + Br- + H2O2
?
-
the formation of bromohydrins by the MPO-H2O2-bromide system using physiological chloride concentrations occurs only at acidic pH values but not at pH 7.4
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + Cl- + H2O2
?
-
the formation of chlorohydrins by the MPO-H2O2-chloride system using physiological chloride concentrations occurs only at acidic pH values but not at pH 7.4
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
? + H2O
-
both properoxinectin and peroxinectin are catalytically active as peroxidases
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
-
-
-
?
Amplex Red + H2O2
resorufin + H2O
i.e. 10-acetyl-2,7-dihydroxyphenoxazine
-
-
?
Br- + H2O2
HBrO + H2O
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at physiological concentrations of chloride and bromide, hypobromous acid can be a major oxidant produced by myeloperoxidase
-
-
?
Cl- + H2O2 + chloroacetonitrile
HClO + H2O + cyanide
-
chloride ion (Cl-) is the dominant electron donor, chloroacetonitrile is activated to cyanide by myeloperoxidase/H2O2/Cl- system in vitro
-
-
?
guaiacol + H2O2
?
-
at neutral pH MPO has higher affinity to peroxidase substrate guaiacol
-
-
?
low-density lipoprotein + Cl- + H2O2
? + H2O
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enzyme produces oxidative modifications of the protein moiety of low density lipoproteins
-
?
myricitrin + H2O2
? + H2O
-
myeloperoxidase is less efficient at oxidizing myricitrin at higher concentrations (0.05 mM) of H2O2
-
-
?
NADH + O2 + H+
NAD+ + H2O2
-
myeloperoxidase is capable of catalyzing an oscillating peroxidase-oxidase reaction, when chloride is present in the reaction mixture
-
-
?
nitrite + L-tyrosine + H2O2 + H+
?
-
poor substrate for myeloperoxidase, but free tyrosine facilitates nitration of tyrosyl residues by acting as a cosubstrate in the reaction
-
-
?
serotonin + H2O2
serotonin dimer + H2O
favoured substrate of myeloperoxidase, only ascorbate blocks oxidation of serotonin
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-
?
Cl- + H2O2 + H+
HClO + H2O
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711123, 711124, 711125, 711274, 711350, 711881, 711882, 711998, 712340, 712342, 712353, 712361, 713436, 741769, 742084, 764118, 764297, 764466
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-
?
Cl- + H2O2 + H+
HClO + H2O
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at acidic pH, chlorinating activity of MPO dominates
-
-
?
Cl- + H2O2 + H+ + taurine + H+
taurine monochloroamine + 2 H2O
-
the taurine chlorination reaction mediated by the myeloperoxidase system in vivo may involve an enzyme intermediate species rather than free HOCl
-
-
?
Cl- + H2O2 + H+ + taurine + H+
taurine monochloroamine + 2 H2O
-
-
-
?
I- + H2O2
?
-
myeloperoxidase plays a fundamental role in oxidant production by neutrophils
-
-
?
I- + H2O2 + H+
HIO + H2O
iodide is a better electron donor for MPO compound I than Br-
-
-
?
thiocyanate + H2O2 + H+
hypothiocyanite + H2O
-
thiocyanate is a major physiological substrate of myeloperoxidase and most favoured substrate compared to chloride and bromide
-
-
?
thiocyanate + H2O2 + H+
hypothiocyanite + H2O
-
thiocyanate is the most favoured substrate compared to chloride and bromide. With 0.1 mM thiocyanate about 50% of the H2O2 present is converted into hypothiocyanite, the rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubles when 0.1 mM thiocyanate is added, and is maximal with 1 mM thiocyanate
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-
?
additional information
?
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-
analysis of kinetics for eosinophil peroxidase and myeloperoxidase
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-
?
additional information
?
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-
myeloperoxidase kills microorganisms via a reaction that involves H2O2 and a halide
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-
?
additional information
?
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-
possible role of the enzyme for neutrophil myeloperoxidase in cystic fibrosis lung disease
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-
?
additional information
?
-
halides serve as substrates or inhibitors, existence of two halide binding sites that have a distinct impact on the heme iron microenvironment in myeloperoxidase
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-
?
additional information
?
-
-
myeloperoxidase mediates protein tyrosine nitration
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-
?
additional information
?
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-
bromide, at physiological concentrations, promotes a dramatic increase in bromination of human serum albumin catalyzed by myeloperoxidase
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-
?
additional information
?
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-
HClO released from the enzyme chlorinates L-Pro-Gly-Gly producing N-chloro-L-Pro-Gly-Gly. L-taurine, a smaller substrate, may be chlorinated in the heme product of the enzyme
-
-
?
additional information
?
-
-
in the presence of physiological concentrations of nitrite and chloride, myeloperoxidase catalyzes little nitration of tyrosyl residues in a heptapeptide. However, the efficiency of nitration is enhanced at least 4fold by free tyrosine. Myeloperoxidase oxidizes free tyrosine to tyrosyl radicals that exchange with tyrosyl residues in peptides. These peptide radicals then couple with nitrogen dioxide to form 3-nitrotyrosyl residues
-
-
?
additional information
?
-
-
in the presence of the complete MPO/H2O2/Cl- system, lyso-products and chlorohydrins are only formed at pH values lower than pH 6.0 with an optimum at pH 4.3
-
-
?
additional information
?
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-
myeloperoxidase generates 3-chlorotyrosine and 3-bromotyrosine during sepsis. In the brominating pathway, myeloperoxidase initially produces HOCl, which reacts with Br2 to generate brominating intermediates. Both chlorination and bromination of N-acetyl-L-tyrosine to N-acetyl-L-3-chlorotyrosine or N-acetyl-L-3-bromotyrosine are optimal under acidic conditions, but significant levels of the halogenated amino acids are also generated at neutral pH. Under acidic (pH 5.9) and neutral conditions, bromination by myeloperoxidase requires both enzyme and H2O2, it is inhibited by catalase (a peroxide scavenger), sodium azide (a heme poison), and taurine (a scavenger of hypohalous acids)
-
-
?
additional information
?
-
-
only amino acids with free amino and carboxylic acid groups on the alpha-carbon yield aldehydes when oxidized by the myeloperoxidase-H2O2-Cl- system. Incubation of the alpha-amino blocked analog Nalpha-acetyllysine with the complete myeloperoxidase system fails to generate detectable aldehyde
-
-
?
additional information
?
-
-
the enzyme is able to degrade carboxylated single-walled carbon nanotubes
-
-
?
additional information
?
-
-
compared with native apolipoprotein A-I, apolipoprotein A-I containing a Y192F mutation is moderately resistant to oxidative inactivation by the enzyme
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-
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