Target intelligence / Profile preview

NAD⁺-dependent enzyme (none (NAD⁺-dependent enzymes is used generically; specific enzymes may have individual abbreviations, such as PARP for poly(ADP-ribose) polymerase, SIRT for sirtuin))

Target
none (NAD⁺-dependent enzymes is used generically; specific enzymes may have individual abbreviations, such as PARP for poly(ADP-ribose) polymerase, SIRT for sirtuin)
Molecular classification
Enzyme, Oxidoreductase, Dehydrogenase, Poly(ADP-ribose) polymerase, ADP-ribosyl cyclase, Sirtuin, Ligase, Mono-ADP-ribosyltransferase, Tankyrase, tRNA-phosphotransferase, Other (the term covers dozens of enzymes across several superfamilies)
01

Overview

NAD⁺-dependent enzymes are a diverse group of enzymes that require nicotinamide adenine dinucleotide (NAD⁺) as a cofactor or substrate for their catalytic activity. They are integral to numerous cellular processes, including redox metabolism, DNA repair, epigenetic regulation, and cell signaling. Major families include oxidoreductases (such as dehydrogenases involved in glycolysis and the TCA cycle), sirtuins (regulators of protein acetylation and aging), poly(ADP-ribose) polymerases (key mediators in DNA damage repair), CD38/CD157 (involved in calcium signaling via cyclic ADP-ribose generation), and others. These enzymes are implicated in many diseases, notably aging-related disorders, cancer, metabolic and cardiovascular diseases, and neurodegeneration. They are therapeutically relevant, with several drug classes targeting specific members for indications like cancer or inflammatory disease. Modulation of NAD⁺-dependent enzyme activity, either through direct inhibition/activation or via adjusting NAD⁺ levels, remains a promising, but complex and context-dependent, area of biomedical intervention. The search query "NAD⁺-dependent enzymes" refers to a *class* of enzymes rather than a single molecular target. This group encompasses hundreds of distinct enzymes across multiple molecular families and biological functions. Therefore, while the term functions as an umbrella for broadly NAD⁺-utilizing enzymes (most of which are indeed therapeutic targets), it is not a unique or canonical single molecule. For structured data, specific enzyme examples—such as "Poly(ADP-ribose) polymerase 1 (PARP1)", "Sirtuin 1 (SIRT1)", or "Nicotinamide phosphoribosyltransferase (NAMPT)"—should be used instead of the group term. If you intend a specific NAD⁺-dependent enzyme, provide its name for single-target mapping.

Other names
NAD-dependent enzymeNAD⁺-consuming enzymeNAD-dependent oxidoreductaseNAD-dependent dehydrogenaseNAD⁺-dependent hydrolaseNAD⁺-regulating enzymeNAD⁺-utilizing enzymeNAD⁺-catabolizing enzyme
02

Mechanism of action

Inhibition of enzyme activity (e.g., blocking PARP to prevent DNA repair in cancer cells); Activation or stabilization of target enzyme (e.g., sirtuin activators promote beneficial deacetylation); Modulation of NAD⁺ biosynthesis or degradation (NAMPT/NNMT inhibitors modulate cellular NAD⁺ levels); Alteration of redox state

03

Biological functions

Redox reactionsEnergy metabolismDNA repairGenomic stabilityGene expression regulationRNA processingCellular signalingCircadian rhythm regulationApoptosisCell proliferationCell deathImmune responseChromatin remodelingVascular functionEpigenetic modification
04

Disease associations

AgingMetabolic diseasesCancerNeurodegenerationCardiovascular diseaseInflammationInfectionChronic diseases of aging
05

Safety considerations

Off-target effects due to broad roles of NAD⁺-dependent enzymesPotential impact on physiological NAD⁺ homeostasis and redox balanceImmunosuppression or exacerbation of inflammationCardiotoxicity and metabolic disruption from inhibition of NAD⁺ biosynthetic pathwaysRisk of accelerating aging phenotypes by interfering with NAD⁺ functionsEffects on genomic stability
06

Interacting drugs

PARP inhibitors (e.g., olaparib, niraparib)

6 more in the full profile.

07

Biomarkers

NAD⁺/NADH ratioActivity or expression of sirtuins, PARPs, NAMPTCirculating NAMPT (as a marker in inflammation/metabolic disease)Levels of NAD⁺ metabolitesDNA repair activity

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