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

BRENDA support

Literature summary for 1.11.2.2 extracted from

  • Wang, Y.; Rosen, H.; Madtes, D.K.; Shao, B.; Martin, T.R.; Heinecke, J.W.; Fu, X.
    Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: an oxidative mechanism for regulating proteolysis during inflammation (2007), J. Biol. Chem., 282, 31826-31834.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
phagocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
MPO
-
Homo sapiens

General Information

General Information Comment Organism
physiological function HOCl generated by the MPO-H2O2-chloride system inactivates tissue inhibitor of metalloproteinase-1 by oxidizing its N-terminal cysteine Homo sapiens