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Literature summary for 1.11.2.2 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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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Organism

Organism UniProt Comment Textmining
Bos taurus
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
spleen
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Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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?

Synonyms

Synonyms Comment Organism
donor: H2O2 oxidoreductase
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Bos taurus