NAD⁺

Nicotinamide Adenine Dinucleotide (NAD⁺) is a fundamental coenzyme in cellular biochemistry, cycling between oxidized (NAD⁺) and reduced (NADH) forms across hundreds of redox reactions. It is also a direct substrate for sirtuin deacylases and poly(ADP-ribose) polymerases (PARPs), placing it at the center of contemporary research on metabolism, chromatin biology, and the DNA damage response. Intracellular NAD⁺ levels decline measurably with age and metabolic stress — an observation that has driven substantial research interest.

As a cofactor, NAD⁺ accepts electrons in dehydrogenase reactions across glycolysis, the TCA cycle, and beta-oxidation, generating NADH which feeds the electron transport chain. As a substrate, NAD⁺ is cleaved by NAD⁺-consuming enzymes — sirtuins (SIRT1–7), CD38, and PARPs — releasing nicotinamide. Sirtuin deacylation activity links cellular NAD⁺ status to chromatin remodeling and metabolic gene expression. PARP-mediated NAD⁺ consumption is upregulated by DNA damage.

Used as a substrate in enzymatic assays (LDH, MDH, alcohol dehydrogenase, sirtuin activity assays), as a metabolic standard in mass spectrometry, and in cellular research on NAD⁺ biosynthetic and salvage pathways. NAD⁺ is one of the most heavily cited substrates across biochemistry literature.

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