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Literature summary for 1.11.2.2 extracted from

  • 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.; Heinecke, J.W.
    Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis (2001), Proc. Natl. Acad. Sci. USA, 98, 11961-11966.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining
HL-60 cell
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Homo sapiens
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neutrophil
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cl- + H2O2 + H+
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Homo sapiens HClO + H2O
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additional information 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) Homo sapiens ?
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General Information

General Information Comment Organism
malfunction mice deficient in myeloperoxidase are more likely than wild type mice to die from infection by polymicrobial sepsis Homo sapiens
physiological function myeloperoxidase protects against sepsis in vivo by producing halogenating species, myeloperoxidase plays an important role in host defense against bacterial pathogens Homo sapiens