NADP-dependent oxidoreductase

NADP-dependent oxidoreductases are a diverse superfamily of enzymes that catalyze oxidation-reduction reactions using nicotinamide adenine dinucleotide phosphate (NADP+/NADPH) as a cofactor (8, 11). These enzymes play fundamental roles in cellular metabolism, including the biosynthesis of essential molecules such as fatty acids, cholesterol, and steroids, as well as the maintenance of the cellular redox state through the regeneration of antioxidants like glutathione (10). Because of their central role in metabolism and signaling, many members of this class, such as dihydrofolate reductase (DHFR) and HMG-CoA reductase, are critical therapeutic targets (1, 13). Drugs targeting these enzymes are used to treat a wide range of conditions, including cancer, hyperlipidemia, and infectious diseases like tuberculosis and malaria (3, 13). However, the ubiquity of these enzymes across various tissues and pathways presents challenges for drug selectivity and can lead to significant side effects or metabolic disruptions (5, 7).

Other names

NADP-dependent oxidoreductasesNADPH-dependent oxidoreductaseNAD(P)H-dependent oxidoreductaseNADPH-dependent dehydrogenaseNADP-dependent dehydrogenase

Inhibition of enzyme activity through competitive binding at the substrate or cofactor (NADPH) site, or through covalent modification, thereby disrupting essential metabolic or signaling pathways.