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Literature summary extracted from

  • Marquez, L.A.; Dunford, H.B.
    Chlorination of taurine by myeloperoxidase. Kinetic evidence for an enzyme-bound intermediate (1994), J. Biol. Chem., 269, 7950-7956.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.2.2 H2O2 inhibition of taurine chlorination by H2O2 becomes significant at about pH 6.6 and higher Bos taurus

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+ + taurine + H+ Bos taurus the taurine chlorination reaction mediated by the myeloperoxidase system in vivo may involve an enzyme intermediate species rather than free HOCl taurine monochloroamine + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.2.2 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.2.2
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.2.2 spleen
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.2 Cl- + H2O2 + H+ + taurine + H+ the taurine chlorination reaction mediated by the myeloperoxidase system in vivo may involve an enzyme intermediate species rather than free HOCl Bos taurus taurine monochloroamine + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.2.2 donor: H2O2 oxidoreductase
-
 Bos taurus