Multiple zinc-binding proteins and enzymes

Multiple zinc-binding proteins and enzymes represent a vast and heterogeneous class of proteins that require zinc ions for their structural integrity, catalytic activity, or regulatory functions [1, 4]. It is estimated that approximately 10% of the human proteome consists of zinc-binding proteins, including major enzyme families such as carbonic anhydrases, matrix metalloproteinases (MMPs), and histone deacetylases (HDACs), as well as thousands of zinc-finger transcription factors [4]. Zinc ions serve as essential cofactors for over 300 enzymes, playing critical roles in DNA synthesis, immune function, and protein synthesis [3]. In a therapeutic context, this target group is often discussed in relation to the mechanism of zinc-based antimicrobials like zinc pyrithione, which increases intracellular zinc to levels that inhibit essential fungal enzymes [2]. Additionally, systemic zinc supplementation is used to restore the function of these proteins in deficiency states, while chelating agents like penicillamine are used to remove excess zinc in metal overload disorders [2, 3]. Dysregulation of zinc homeostasis is linked to various pathologies, including growth retardation, immune deficiency, and neurodegenerative diseases [3, 4].

Other names

Zinc-binding proteomeZinc-dependent enzymesZinc-metalloproteinsZinc-binding proteins

Zinc ions act as essential catalytic or structural cofactors for a wide array of proteins; therapeutic agents either provide zinc to restore function or sequester it via chelation to inhibit protein activity [2, 3].