Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.11.2.2 Homo sapiens P05164
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.2.2 neutrophil
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.11.2.2 donor:H2O2 oxidoreductase
-
Homo sapiens
1.11.2.2 MPO
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.2.2 heme
-
Homo sapiens

General Information

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