Multiple enzymes requiring zinc as cofactor

This entry describes a large and heterogeneous group of enzymes that require zinc ions as cofactors for their catalytic activity. Examples include alcohol dehydrogenase, carboxypeptidases, alkaline phosphatase, superoxide dismutase, carbonic anhydrase, matrix metalloproteinases, and angiotensin-converting enzyme. Zinc-dependent enzymes play critical roles in numerous biochemical pathways, including metabolism, signal transduction, cell proliferation, protein digestion, tissue remodeling, and immune regulation. Therapeutically, individual zinc-dependent enzymes (such as ACE or MMPs) serve as drug targets for diseases like hypertension, cancer, and arthritis. However, the entry "multiple enzymes requiring zinc as cofactor" is overly broad and does not refer to a distinct molecular entity, gene, or protein family suitable as a singular drug target; instead, drugs and biomarkers are enzyme-specific. Interference with zinc metabolism or zinc-dependent enzyme activity carries risk for widespread side effects due to zinc's essential role in cellular function. To obtain structured, actionable information, it is necessary to specify individual zinc-dependent enzymes rather than using this umbrella term.

Other names

Zinc-dependent enzyme(s)Zinc metalloenzyme(s)Zinc hydrolase(s)

Inhibition of catalytic activity by blocking the zinc binding site (common for many zinc enzyme inhibitors); Chelation of zinc ions (reducing enzyme activity, used in toxin exposures or experimental inhibition); Competitive inhibition at substrate binding site