Literature summary for 3.4.24.35 extracted from

Xu, X.; Chen, Z.; Wang, Y.; Yamada, Y.; Steffensen, B.
Functional basis for the overlap in ligand interactions and substrate specificities of matrix metalloproteinases-9 and -2 (2005), Biochem. J., 392, 127-134.

Search for more literature for 3.4.24.35

Protein Variants

Protein Variants	Comment	Organism
E402A	no enzymic activity, competition with isolated collagen-binding domain and with matrix metalloproteinase MMP-2 binding to native and denatured type I collagen	Homo sapiens
additional information	recombinant enzyme collagen-binding domain, competition with binding to gelatin of either enzyme mutant E402A or matrix metalloproteinase MMP-2 mutant E404A	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
20947	-	x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain	Homo sapiens
70795	-	x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain	Homo sapiens

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Release 2023.1 (January 2023)