Zinc-dependent enzyme and protein

**Zinc-dependent enzymes and proteins** encompass a vast group of structurally unrelated molecules that require zinc ions for their biological activity and/or stable conformation. Zinc serves as a vital cofactor for over 300 enzymes, including hydrolases (e.g., carbonic anhydrase, matrix metalloproteinases), oxidoreductases (e.g., alcohol dehydrogenase), and ligases, as well as for protein domains such as zinc fingers, which mediate DNA, RNA, and protein interactions[2][5][7][1]. These proteins participate in many essential cellular functions, such as metabolism, gene regulation, cell signaling, apoptosis, and immune responses. The pleiotropic effects and clinical significance of zinc-dependent enzymes have led to their targeting by various drug classes, but the broad biological roles of zinc pose challenges for achieving specificity and minimizing adverse effects[2][4][8]. Disruption in the activity or regulation of zinc-dependent proteins is implicated in numerous diseases, including cancer, cardiovascular, neurodegenerative, and infectious diseases[2][4][6]. **Note:** The entry "Zinc-dependent enzymes and proteins" is too broad and describes a large superfamily rather than a specific, unique molecular target as required for structured pharmacological databases; individual targets (e.g., "Matrix metalloproteinase-9", "Angiotensin-converting enzyme", "Zinc finger protein Egr1") should be specified for precise annotations.

Other names

Zinc enzymeZinc proteinMetalloenzyme (zinc)Zinc-binding protein

Enzyme inhibition (competitive, non-competitive, chelation); Disruption of zinc finger-DNA interactions; Modulation of protein conformation and activity via zinc binding or chelation; Inhibition of proteolytic activity of metalloproteinases