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Literature summary extracted from

  • Sires, U.I.; Murphy, G.; Baragi, V.M.; Fliszar, C.J.; Welgus, H.G.; Senior, R.M.
    Matrilysin is much more efficient than other matrix metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin (1994), Biochem. Biophys. Res. Commun., 204, 613-620.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.23 carboxylate
-
Mammalia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.23 additional information Mammalia apart from its activity against extracellular matrix, the enzyme provides a mechanism for the regulation of leukocyte elastase activity through its capacity to degrade alpha1-antitrypsin ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.23 Mammalia
-
expressed in NSO mouse myeloma cells
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.23 alpha1-antitrypsin + H2O a single cleavage at the Phe352-Leu353 peptide bond, a locus within active-site loop produces 2 fragments of approximately 50000 MW and 4000 MW Mammalia ?
-
?
3.4.24.23 additional information apart from its activity against extracellular matrix, the enzyme provides a mechanism for the regulation of leukocyte elastase activity through its capacity to degrade alpha1-antitrypsin Mammalia ?
-
?