Copper-dependent enzymes and metalloproteins

Copper-dependent enzymes and metalloproteins, collectively known as cuproenzymes, are a diverse group of proteins that utilize copper as a critical cofactor for their catalytic activity or structural stability [1.1.2, 1.3.1]. These proteins play essential roles in fundamental biological processes, including cellular respiration (cytochrome c oxidase), antioxidant defense (superoxide dismutase 1), connective tissue formation (lysyl oxidase), and neurotransmitter synthesis (dopamine beta-hydroxylase) [1.2.2, 1.3.3]. Dysregulation of copper homeostasis or mutations in these enzymes are linked to various pathologies, such as Menkes and Wilson's diseases, neurodegenerative disorders like ALS and Alzheimer's, and cancer progression [1.2.1, 1.5.1]. Therapeutic strategies targeting this class include copper chelators to reduce enzyme activity in cancer and inflammation, and copper ionophores like elesclomol to induce a novel form of cell death called cuproptosis or to restore mitochondrial function in deficiency states [1.4.1, 1.5.2]. Monitoring these targets often involves measuring serum copper, ceruloplasmin levels, or specific enzyme activities, while safety concerns primarily revolve around maintaining the delicate balance of systemic copper to avoid both deficiency-induced organ failure and toxicity-driven oxidative damage [1.3.1, 1.5.3].

Other names

CuproenzymesCuproproteinsCopper-binding proteinsCopper-containing enzymes

Copper chelation to inhibit enzyme activity, copper ionophore-mediated induction of cuproptosis, restoration of mitochondrial enzyme function through copper delivery, and direct inhibition of specific cuproenzymes.