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Literature summary for 1.11.2.2 extracted from

  • Furtmuller, P.G.; Burner, U.; Obinger, C.
    Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate (1998), Biochemistry, 37, 17923-17930.
    View publication on PubMed
Search for more literature for 1.11.2.2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Cl- + H2O2 + H+ Homo sapiens
-
 HClO + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P05164
-
-

Source Tissue

Source Tissue Comment Organism Textmining
neutrophil
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Br- + H2O2 + H+
-
 Homo sapiens HBrO + H2O
-
 ?
Cl- + H2O2 + H+
-
 Homo sapiens HClO + H2O
-
 ?
I- + H2O2 + H+ iodide is a better electron donor for MPO compound I than Br- Homo sapiens HIO + H2O
-
 ?
thiocyanate + H2O2 + H+
-
 Homo sapiens hypothiocyanate + H2O
-
 ?

Synonyms

Synonyms Comment Organism
donor:H2O2 oxidoreductase
-
 Homo sapiens
MPO
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function myeloperoxidase plays a fundamental role in oxidant production by neutrophils Homo sapiens