Literature summary for 3.4.24.80 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.

Search for more literature for 3.4.24.80

Cloned(Commentary)

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

Inhibitors

Inhibitors	Comment	Organism	Structure
AGN3340	-	Homo sapiens
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
additional information	no inhibitor: TIMP-1	Homo sapiens
TIMP-2	tissue inhibitor of metalloproteinases	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P50281	-	-

Purification (Commentary)

Purification (Comment)	Organism
catalytic domain	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha1-antitrypsin + H2O	-	Homo sapiens	?	-	?
progelatinase A + H2O	syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A	Homo sapiens	?	-	?
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	?	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)