Zinc-dependent metalloprotease

Zinc-dependent metalloproteases are a diverse class of enzymes that utilize a catalytic zinc ion at their active site to hydrolyze peptide bonds, chiefly within proteins of the extracellular matrix such as collagen. The zinc ion is usually held in a conserved motif by several histidine and glutamate residues, with a water molecule positioned for nucleophilic attack on the peptide substrate[1][3][5][7][8]. These enzymes play key roles in tissue remodeling, development, immune response, and pathologic processes such as cancer metastasis and bacterial toxin action. Despite many attempts, selective drug targeting has been challenging due to their structural similarity and broad physiological roles. This target name refers to an entire class, not one single protein, and should be specified further for precise therapeutic or research purposes.

Other names

MetalloproteaseMetalloproteinaseMatrix metalloproteinase (for specific subfamily)ADAMADAMTSMMP (for matrix metalloproteinases)

Inhibition of proteolytic activity (by chelating active-site zinc or blocking substrate binding sites) Regulation or prevention of ECM degradation Interference with cell signaling by preventing target cleavage