Literature summary extracted from

Rozanov, D.V.; Ghebrehiwet, B.; Postnova, T.I.; Eichinger, A.; Deryugina, E.I.; Strongin, A.Y.
The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR (2002), J. Biol. Chem., 277, 9318-9325.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.4.24.80	two truncated forms: CAT domain and CAT/PEX domain	Homo sapiens

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.4.24.80	AGN3340	-	Homo sapiens
3.4.24.80	GM6001	hydroxamate inhibitor, 0.001 mM, converts protease into a cell surface receptor for receptor of complement component 1q and promotes co-precipitation of the enzyme with the soluble receptor protein	Homo sapiens
3.4.24.80	additional information	no inhibitor: TIMP-1	Homo sapiens
3.4.24.80	TIMP-2	tissue inhibitor of metalloproteinases	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.24.80	Homo sapiens	P50281	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.4.24.80	catalytic domain	Homo sapiens

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.4.24.80	alpha1-antitrypsin + H2O	-	Homo sapiens	?	-	?
3.4.24.80	progelatinase A + H2O	syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A	Homo sapiens	?	-	?
3.4.24.80	receptor of complement component 1q + H2O	cleaves at Gly79-Gln80, cleavage with CAT/PEX domain leads to fragments with the following MW: 17 kDa, 12 kDa and 11 kDa	Homo sapiens	?	-	?

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Release 2023.1 (January 2023)