321-02-8 Usage
Description
Nicotinic Acid Mononucleotide (NaMN) is a nucleotide derived from nicotinic acid, which is produced from quinolinic acid by quinolinate phosphoribosyltransferase through the transfer of a phosphoribose group. It serves as an intermediate in the biosynthesis of Nicotinic Acid Adenine Dinucleotide (NaAD) and is further converted to NAD via amidation. NAD is then transformed into NADPH, playing a crucial role in cellular metabolism and energy production.
Uses
Used in Pharmaceutical Industry:
Nicotinic Acid Mononucleotide is used as an intermediate for the production of NAD and NADPH, which are essential coenzymes involved in various cellular processes, including energy metabolism, redox reactions, and cellular signaling. These coenzymes have potential applications in the development of therapeutics for a range of diseases, such as mitochondrial disorders, neurodegenerative diseases, and metabolic disorders.
Used in Nutritional Supplements:
NaMN is used as a dietary supplement to support the body's natural production of NAD and NADPH. These coenzymes are known to play a role in maintaining cellular health, promoting energy metabolism, and supporting the immune system. As a supplement, NaMN may help improve overall health and well-being.
Used in Research and Development:
Nicotinic Acid Mononucleotide is used as a research tool in the study of cellular metabolism, enzyme function, and the role of NAD and NADPH in various biological processes. It can be employed in the development of novel therapeutic strategies and the investigation of the underlying mechanisms of various diseases.
Used in Cosmetics Industry:
NaMN may also find applications in the cosmetics industry, where it could be used as an ingredient in anti-aging and skin health products. The role of NAD and NADPH in cellular metabolism and redox balance may contribute to the maintenance of healthy skin and the reduction of visible signs of aging.
Check Digit Verification of cas no
The CAS Registry Mumber 321-02-8 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 3,2 and 1 respectively; the second part has 2 digits, 0 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 321-02:
(5*3)+(4*2)+(3*1)+(2*0)+(1*2)=28
28 % 10 = 8
So 321-02-8 is a valid CAS Registry Number.
InChI:InChI=1/C11H14NO9P/c13-8-7(5-20-22(17,18)19)21-10(9(8)14)12-3-1-2-6(4-12)11(15)16/h1-4,7-10,13-14H,5H2,(H2-,15,16,17,18,19)/p+1/t7-,8-,9-,10-/m1/s1
321-02-8Relevant articles and documents
Dissecting cobamide diversity through structural and functional analyses of the base-activating CobT enzyme of Salmonella enterica
Chan, Chi Ho,Newmister, Sean A.,Talyor, Keenan,Claas, Kathy R.,Rayment, Ivan,Escalante-Semerena, Jorge C.
, p. 464 - 475 (2014)
Background Cobamide diversity arises from the nature of the nucleotide base. Nicotinate mononucleotide (NaMN):base phosphoribosyltransferases (CobT) synthesize α-linked riboside monophosphates from diverse nucleotide base substrates (e.g., benzimidazoles, purines, phenolics) that are incorporated into cobamides. Methods Structural investigations of two members of the CobT family of enzymes in complex with various substrate bases as well as in vivo and vitro activity analyses of enzyme variants were performed to elucidate the roles of key amino acid residues important for substrate recognition. Results Results of in vitro and in vivo studies of active-site variants of the Salmonella enterica CobT (SeCobT) enzyme suggest that a catalytic base may not be required for catalysis. This idea is supported by the analyses of crystal structures that show that two glutamate residues function primarily to maintain an active conformation of the enzyme. In light of these findings, we propose that proper positioning of the substrates in the active site triggers the attack at the C1 ribose of NaMN. Conclusion Whether or not a catalytic base is needed for function is discussed within the framework of the in vitro analysis of the enzyme activity. Additionally, structure-guided site-directed mutagenesis of SeCobT broadened its substrate specificity to include phenolic bases, revealing likely evolutionary changes needed to increase cobamide diversity, and further supporting the proposed mechanism for the phosphoribosylation of phenolic substrates. General Significance Results of this study uncover key residues in the CobT enzyme that contribute to the diversity of cobamides in nature.
