NAAD sodium salt
NAAD sodium salt structure
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Common Name | NAAD sodium salt | ||
|---|---|---|---|---|
| CAS Number | 104809-30-5 | Molecular Weight | 686.39 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C21H25N6NaO15P2 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme.
Mol. Cell. 17 , 855-868, (2005) Sir2 enzymes form a unique class of NAD(+)-dependent deacetylases required for diverse biological processes, including transcriptional silencing, regulation of apoptosis, fat mobilization, and lifespan regulation. Sir2 activity is regulated by nicotinamide, a... |
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Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.
Structure 10 , 69-79, (2002) Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target fo... |
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Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry.
Biochemistry 42 , 9249-9256, (2003) Life span regulation and inhibition of gene silencing in yeast have been linked to nicotinamide effects on Sir2 enzymes. The Sir2 enzymes are NAD(+)-dependent protein deacetylases that influence gene expression by forming deacetylated proteins, nicotinamide a... |
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Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements.
J. Biol. Chem. 280 , 15131-15140, (2005) Nicotinamide adenine dinucleotide synthetases (NADS) catalyze the amidation of nicotinic acid adenine dinucleotide (NAAD) to yield the enzyme cofactor nicotinamide adenine dinucleotide (NAD). Here we describe the crystal structures of the ammonia-dependent ho... |
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Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 , 893-898, (2008) Nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC 2.7.7.18) is the penultimate enzyme in the biosynthesis of NAD(+) and catalyzes the adenylation of nicotinic acid mononucleotide (NaMN) by ATP to form nicotinic acid adenine dinucleotide (NaAD). Th... |