Nicotinamide - CAS 98-92-0
Catalog number: 98-92-0
Category: Inhibitor
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Nicotinamide, a water-soluble vitamin, is an active component of coenzymes NAD and NADP, and also act as an activator of sirtuins.
Vitamin B3
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1. Photoprotective effects of nicotinamide
Diona L. Damian*. Photochem. Photobiol. Sci., 2010, 9, 578–585
Nicotinamide intake, deficiency and pharmacology Nicotinamide and nicotinic acid (niacin, which is converted to nicotinamide in vivo; Fig. 1) are most abundant in foods such as meats, legumes, nuts, grains, coffee and tea, andinniacin-fortified cereals. Nicotinamide is also manufactured in the liver from tryptophan, which is found in eggs, dairy products, fish, meat and soybeans and comprises up to 2% of total dietary protein. The tryptophan pathway provides ~50%of total niacin requirements. Recommended daily nicotinamide intake for adults is ~15 mg, and typical commercially available daily supplement doses range from 20–500 mg.
2. Sirtuin mechanism and inhibition: explored with Ne-acetyl-lysine analogs
Brett M. Hirsch and Weiping Zheng*. Mol. BioSyst., 2011, 7, 16–28
Multiple transcriptional coactivators such as p300, cAMP-response element binding protein (CREB) binding protein (CBP), and p300/CBP-associated factor (PCAF) were shown to possess an intrinsic protein acetyltransferase activity. The yeast transcriptional repressors reduced potassium dependency 3 (Rpd3), histone deacetylase 1 (Hda1), and silent information regulator 2 (Sir2) were shown to possesses a protein deacetylase activity. While acetyl-coenzyme A (AcCoA) is used as the universal cofactor to donate the acetyl group during lysine Ne-acetylation catalyzed by all the protein acetyltransferases, the enzymatic lysine Ne-deacetylation is accomplished by the deacetylase enzymes that use either Zn2+ or b-nicotinamide adenine dinucleotide (β-NAD+ or just NAD+ as used below throughout this article) as the catalytic cofactor. While the Zn2+-containing metallo-deacetylases catalyze the Zn2+-assisted hydrolysis of the amide bond of the acetyl-lysine side chain to afford the deacetylated product and acetic acid, the NAD+-dependent deacetylases achieve the deacetylation of the acetyl-lysine side chain by catalyzing the ultimate transfer of the acetyl group onto the 2’-OH of the nicotinamide ribose of NAD+, which is coupled to the cleavage of nicotinamide from NAD+, thus affording three enzymatic products, i.e. nicotinamide, the deacetylated product, and 2’-O-acetyl-ADP-ribose (20 -O-AADPR) (Fig. 1). Rpd3 and Hda1 are the two founding members of the Zn+-containing protein deacetylase enzyme family that also includes the eleven human homologs (HDAC1-11, HDAC stands for histone deacetylase). Sir2 is the founding member of the NAD+-dependent protein deacetylase enzyme family that is also known as the sirtuin family.
3. Protection effect of nicotinamide on cardiomyoblast hypoxia/re-oxygenation injury: study of cellular mitochondrial metabolism
He Wang, Xiaoping Liang,* Guoan Luo, Mingyu Ding and Qionglin Liang*. Mol. BioSyst., 2016, 12, 2257—2264
Nicotinamide, the amide form of nicotinic acid, is the precursor of the coenzymeβNAD, which is an important currency for cell energy metabolism. The protective properties of nicotinamide in enhancement of cell survival as well as longevity, especially in neuroprotection, have been widely discussed. It has been proved to be neuroprotective by poly(ADP-ribose)polymerase inhibition and lipid peroxidation. Furthermore, a nicotinamide-rich diet could up-regulate SUR2A and ATP-sensitive K+ channels in H/R injured mice, thus increasing cardiac resistance to H/R. It has also been proved that nicotinamide could increase the membrane potential of mitochondria, thus improving mitochondrial stress in cardiomyocytes. However, little is known about the role of nicotinamide in metabolism regulation during cardiac H/R injury. We suppose that nicotinamide may preserve mitochondrial NAD-linked respiration and regulate cellular metabolism, especially the mitochondrial metabolism (Fig. 1).
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CAS 98-92-0 Nicotinamide

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