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Literature summary for 3.4.24.23 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
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Inhibitors

Inhibitors Comment Organism Structure
carboxylate
-
 Mammalia

Natural Substrates/ Products (Substrates)

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

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

Substrates and Products (Substrate)

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