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NAD+ is nicotinamide adenine dinucleotide, a dinucleotide cofactor present in every living cell. It is a coenzyme, not a peptide: two nucleotides, one carrying nicotinamide and one carrying adenine, joined through a pair of phosphate groups. It belongs to the pyridine-nucleotide coenzyme class.
In the published preclinical literature, NAD+ has been characterised at the molecular level as the cofactor and substrate of the enzymes that read and consume it. Cell-free structural and enzymology work has resolved how a Sir2-family NAD+-dependent deacetylase couples hydrolysis of the dinucleotide to removal of an acetyl group, forming nicotinamide and O-acetyl-ADP-ribose, and how a CD38 glycohydrolase cleaves the nicotinamide-ribose bond of NAD+ through trapped catalytic intermediates. It is supplied as a research compound and is not intended for human or veterinary use.
NAD+ has been characterised in preclinical laboratory models as the cofactor and substrate of the enzymes that process it. The primary studies below, in cell-free structural and enzymology assays, measured how a Sir2-family NAD+-dependent deacetylase couples hydrolysis of the dinucleotide to substrate deacetylation, and how a CD38 glycohydrolase cleaves NAD+ through trapped catalytic intermediates. The literature is preclinical; it describes the compound, not any outcome in humans.
In vitro
Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone and protein deacetylases
In cell-free assays with purified yeast Sir2, yeast HST2, and SIRT2 against acetylated histone peptides, the study measured the kinetic mechanism that couples NAD+ hydrolysis to deacetylation and resolved the individual chemical steps forming nicotinamide and O-acetyl-ADP-ribose as the measured endpoint.
Read the study ↗
In vitro
Structural insights into intermediate steps in the Sir2 deacetylation reaction
By X-ray crystallography of the bacterial sirtuin Sir2Tm captured with substrate analogues, the study resolved intermediate chemical steps of the NAD+-dependent deacetylation reaction, mapping how the dinucleotide is positioned and processed in the catalytic pocket as a structural endpoint.
Read the study ↗
Full documentation, on the record. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product.
