NAD+

Molecular Profile

Type

Pyridine-dinucleotide coenzyme

Molecular formula

C21H27N7O14P2

Molecular weight

663.43 g/mol

CAS number

53-84-9

Mechanism & Target Class

NAD+ operates through two broad biochemical modes. As a redox cofactor, it accepts a hydride at the C4 position of its nicotinamide ring to form NADH — a reversible reaction exploited by hundreds of oxidoreductases and dehydrogenases that bind it through a conserved βαβ Rossmann-fold dinucleotide-binding motif. As a consumable cosubstrate, NAD+ is cleaved at the glycosidic bond between nicotinamide and the ADP-ribose moiety by three signaling-enzyme families: poly(ADP-ribose) polymerases (PARPs/ARTDs), which transfer ADP-ribose units onto acceptor proteins in DNA-damage responses; sirtuins (SIRT1–7), NAD+-dependent protein deacylases that couple acyl-lysine mark removal to production of nicotinamide and 2′-O-acyl-ADP-ribose; and NAD+ glycohydrolases/ADP-ribosyl cyclases (CD38, CD157/BST1, and the TIR-domain NADase SARM1). Cellular NAD+ pools are compartmentalized across the cytosol, nucleus, and mitochondria, with SLC25A51 identified as a mammalian mitochondrial NAD+ transporter.

Storage & Handling

Lyophilized

-20°C long term; store desiccated, sealed from air, and protected from light. NAD+ is hygroscopic.

Handling

Hygroscopic in solid state; aqueous NAD+ is labile and degrades with heat, alkaline pH, and repeated freeze-thaw. Aliquot working solutions to limit hydrolysis.

Primary Database

PubChem CID 5892 ↗

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