Systemic zinc-dependent enzymes and proteins (None)

Systemic zinc-dependent enzymes and proteins represent a broad class of biomolecules that utilize zinc ions for catalytic, structural, or regulatory purposes. It is estimated that approximately 10% of the human proteome consists of zinc-binding proteins, highlighting their essential role in physiology (Andreini et al., 2006). These include major enzyme families such as carbonic anhydrases, matrix metalloproteinases (MMPs), and histone deacetylases (HDACs), as well as structural motifs like zinc fingers found in transcription factors (McCall et al., 2000). Biologically, these proteins are involved in diverse processes ranging from DNA replication and gene expression to signal transduction and extracellular matrix remodeling. Due to their widespread involvement in cellular functions, dysregulation of specific zinc-dependent proteins is linked to diseases such as cancer, cardiovascular disorders, and neurodegeneration (Vallee & Auld, 1990). While many individual members of this group are validated therapeutic targets, the group as a whole is too heterogeneous to be considered a single target. Pharmacological intervention typically involves small molecules that coordinate with the zinc ion in the active site, though lack of specificity across the zinc proteome remains a significant safety challenge (Maret, 2013).

Other names

Zinc-binding proteinsZinc proteomeZinc metalloenzymesZinc-dependent proteins

Drugs targeting these proteins typically function by chelating the catalytic zinc ion or by occupying the active site to prevent substrate binding (Maret, 2013).