Nicotinamide adenine dinucleotide-dependent dehydrogenase (NAD-dependent dehydrogenase)

NAD-dependent dehydrogenases represent a vast and diverse class of oxidoreductase enzymes that catalyze the transfer of a hydride ion from a substrate to the coenzyme nicotinamide adenine dinucleotide (NAD+), or vice versa. These enzymes are fundamental to cellular metabolism, playing critical roles in pathways such as glycolysis, the tricarboxylic acid (TCA) cycle, and fatty acid oxidation. By modulating the NAD+/NADH ratio, they serve as key regulators of the cell's redox state and energy production. In a clinical context, specific members of this family are targeted for various therapeutic purposes; for example, aldehyde dehydrogenase is targeted by disulfiram for alcohol aversion therapy, and lactate dehydrogenase is often investigated as a target in cancer metabolism. However, the term "General NAD-dependent dehydrogenases" is considered too broad for a specific drug target, as it encompasses hundreds of distinct enzymes with varying substrates and physiological roles. Therapeutic intervention typically requires high specificity to avoid widespread metabolic disruption and systemic toxicity associated with inhibiting such a fundamental class of enzymes.

Other names

NAD-linked dehydrogenaseNAD-dependent oxidoreductaseNicotinamide adenine dinucleotide-linked oxidoreductase

Inhibition of enzymatic activity by competing with the NAD+ substrate or binding to the active site to prevent the oxidation of specific substrates.