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

BRENDA support

Literature summary for 1.11.2.2 extracted from

  • Kubala, L.; Kolarova, H.; Vitecek, J.; Kremserova, S.; Klinke, A.; Lau, D.; Chapman, A.L.; Baldus, S.; Eiserich, J.P.
    The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix (2013), Biochim. Biophys. Acta, 1830, 4524-4536.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Homo sapiens
-
leukocyte
-
Homo sapiens
-

General Information

General Information Comment Organism
physiological function enzyme binds to the extracellular matrix proteins collagen IV and fibronectin, and this association is enhanced by the pre-incubation of these proteins with glycosaminoglycans. Correspondingly, an excess of glycosaminoglycans in solution during incubation inhibits the binding of enzyme to collagen IV and fibronectin. The oxidizing and chlorinating potential of myeloperoxidase is preserved upon binding to collagen IV and fibronectin, even the potentiation of enzyme activity in the presence of collagen IV and fibronectin is observed Homo sapiens