NAD+: research summary
For laboratory research use only. Not for human or veterinary use. This page summarises published literature. It gives no advice on use.
What the literature covers
NAD+ (nicotinamide adenine dinucleotide, oxidised form) is not a peptide. It is a dinucleotide coenzyme that carries electrons in redox reactions and is consumed as a substrate by sirtuins and PARP enzymes.
Classic biochemistry measured the free NAD+/NADH redox state in the cytoplasm and mitochondria. Later work linked NAD+ availability to SIRT1 deacetylase activity and to AMPK signalling. NAD+ is a standard reagent in enzymology and metabolism research.
Its molecular weight is about 663.4 g/mol (C21H27N7O14P2). It is hygroscopic and light-sensitive, so keep it sealed and protected from moisture.
Key facts
| NAD+ | MOTS-c | |
|---|---|---|
| CAS | 53-84-9 | 1627580-64-6 |
| Formula | C21H27N7O14P2 | C101H152N28O22S2 |
| Molecular weight (g/mol) | 663.4 | 2174.6 |
Source: PubChem CID 5892.
NAD+ compared with MOTS-c
NAD+ is often listed next to peptides, but it is a small-molecule coenzyme, whereas MOTS-c is a 16-residue peptide. Both appear in metabolism and mitochondrial research, but the experiments differ: NAD+ is used as an enzyme substrate and cofactor, while MOTS-c is studied as a signalling peptide.
Full side-by-side: NAD+ vs MOTS-c · MOTS-c research summary
Frequently asked questions
- Is NAD+ a peptide?
- No. It is a dinucleotide coenzyme made of two nucleotides joined through their phosphate groups.
- Which enzymes use NAD+?
- Dehydrogenases use it as an electron carrier. Sirtuins (such as SIRT1) and PARPs consume it as a substrate.
- How should NAD+ be stored?
- Sealed, dry, cold and out of light. It absorbs moisture readily.
Published literature cited
- Cantó C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, Milne JC, Elliott PJ, Puigserver P, Auwerx J. (2009). AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature. PMID 19262508 · doi:10.1038/nature07813
- Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, Pandita TK, Guarente L, Weinberg RA. (2001). hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell. PMID 11672523 · doi:10.1016/s0092-8674(01)00527-x
- Williamson DH, Lund P, Krebs HA. (1967). The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J. PMID 4291787 · doi:10.1042/bj1030514
- Cantó C, Menzies KJ, Auwerx J. (2015). NAD(+) Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus. Cell Metab. PMID 26118927 · doi:10.1016/j.cmet.2015.05.023
Every citation was looked up by PMID in Europe PMC (MEDLINE) on 2026-10-14 and its title matched. Citation means the paper exists and is relevant to the compound. It does not mean the paper supports any use.