Zincmetallopeptidaser

Zincmetallopeptidaser is not a standard term in enzymology, but it most closely corresponds to zinc metallopeptidases, a broad class of zinc-dependent proteases that hydrolyze peptide bonds in proteins. These enzymes are metalloendopeptidases that rely on a catalytic zinc ion in the active site to polarize a water molecule, which then acts as a nucleophile to attack the peptide bond.

The active site typically features coordinating histidine residues and often a carboxylate residue that helps position the zinc ion. A conserved motif, such as HEXXH, is common in many families of zinc metallopeptidases and contributes to zinc binding and catalysis. Subtle variations in active-site architecture and surrounding domains give rise to diverse substrate specificities and regulatory properties.

Zinc metallopeptidases are found in many cellular contexts and can be secreted, membrane-anchored, or intracellular. Major groups include the metzincins, such as matrix metalloproteinases (MMPs) and the ADAM/ADAMTS families, as well as astacins and other related enzymes. They participate in tissue remodeling, extracellular matrix turnover, processing of bioactive peptides, and protein maturation. Their activity is tightly regulated at multiple levels, including transcription, zymogen activation, and inhibition by endogenous inhibitors like tissue inhibitors of metalloproteinases (TIMPs).

Dysregulation of zinc metallopeptidases is linked to various diseases, including cancer, arthritis, cardiovascular disorders, and neurodegeneration. Therapeutic approaches have explored metalloprotease inhibitors, though clinical success has been limited by specificity and side effects. Understanding their structure–function relationships continues to be important for insights into normal physiology and disease mechanisms.