Metalloenzyme (Human)

Human metalloenzymes are a superfamily of enzymes that require one or more tightly bound metal ions (such as zinc, iron, copper, manganese, nickel, cobalt, or molybdenum) for their catalytic activity or structural integrity. These enzymes are essential for a vast array of biological processes, including redox chemistry (e.g., cytochrome P450s, superoxide dismutase), hydrolysis (e.g., matrix metalloproteinases, carbonic anhydrase), and DNA/protein modification (e.g., zinc finger nucleases). Metalloenzymes are frequent drug targets in many disease settings, but the term "human metalloenzymes" encompasses many distinct enzymes—each with specific functions, disease relevance, and therapeutic challenges[1][2][4][5][6][7]. This term is *not* a precise molecular target but a broad category. For drug discovery, diagnosis, or detailed research, it is necessary to refer to individual metalloenzymes (e.g., "Matrix metalloproteinase 9," "Carbonic anhydrase II," "Zinc finger protein 1") rather than this collective label.

Other names

Metal-dependent enzymeMetal-activated enzyme

Chelation/inhibition of the active site metal ion Competitive inhibition at the substrate binding site Allosteric modulation via metal ion interaction Disruption of metal ion delivery or incorporation