The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
The precursor is cleaved by a furin endopeptidase.
Belongs to the peptidase M10A family.
Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.
Matrix metalloproteinase-15, MMP-15, Membrane-type matrix metalloproteinase 2, Membrane-type-2 matrix metalloproteinase, SMCP-2, MT-MMP 2, MTMMP2, MT2-MMP, MT2MMP, MMP15
Proteins
Immunology & Infectious Disease
75807Da
We found 1 product in 1 category