Niacin-dependent enzyme (null)

Niacin-dependent enzymes comprise a diverse set of more than 400 enzymes that rely on niacin-derived cofactors, NAD and NADP, for their function in redox reactions and metabolic pathways across all tissues[1][2][6]. Major classes include dehydrogenases (central to energy metabolism), poly(ADP-ribose) polymerases (in DNA repair), sirtuins (in gene regulation and aging), ADP-ribosyltransferases, and transferases such as nicotinamide N-methyltransferase[1][3][5]. These enzymes underpin processes such as energy production, DNA repair, cell differentiation, and lipid synthesis, and have roles in disease areas ranging from cardiovascular disease and cancer to neurodegeneration and metabolic disorders. Niacin, through its coenzyme forms, is thus indispensable for cellular health, and dysregulation or deficiency in these pathways can contribute to a variety of pathologies. Therapeutically, these enzyme families are targeted for conditions like hyperlipidemia (niacin), cancer (PARP inhibitors), and aging, but their essentiality and broad activity pose safety and efficacy challenges for drug development and clinical management[1][2][5][6].

Other names

NAD-dependent enzymeNADP-dependent enzymeNiacin coenzyme-dependent enzyme

Substrate or cofactor provision (niacin-derived coenzymes required for enzymatic activity). Redox reactions (transfer of electrons in metabolic pathways). ADP-ribosylation (protein post-translational modification by PARPs). Deacetylation (sirtuins, affecting gene regulation and metabolism). Methylation (NNMT modulates cellular methylation and NAD levels). Anabolic and catabolic reactions (energy metabolism, cholesterol/fatty acid synthesis).