Nicotinamide adenine dinucleotide phosphate

Nicotinamide adenine dinucleotide phosphate
Identifiers
CAS Number	53-59-8 ;
3D model (JSmol)	Interactive image;
ChEBI	CHEBI:44409 ;
ChEMBL	ChEMBL2364573 ;
ChemSpider	5674 ;
ECHA InfoCard	100.000.163
MeSH	NADP
PubChem CID	5885;
UNII	BY8P107XEP ;
	InChI InChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 Key: XJLXINKUBYWONI-NNYOXOHSSA-N ; InChI=1/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 Key: XJLXINKUBYWONI-NNYOXOHSBN;
	SMILES O=C(N)c1ccc[n+](c1)[C@H]2[C@H](O)[C@H](O)[C@H](O2)COP([O-])(=O)OP(=O)(O)OC[C@H]3O[C@@H](n4cnc5c4ncnc5N)[C@@H]([C@@H]3O)OP(=O)(O)O;
Properties
Chemical formula	C21H28N7O17P3+ (oxidized); C21H29N7O17P3 (reduced)
Molar mass	744.4 g/mol (oxidized); 745.4 g/mol (reduced)
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). verify (what is ?) Infobox references

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP^[1]^[2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP⁺ is the oxidized form. NADP⁺ is used by all forms of cellular life. NADP⁺ is essential for life because it is needed for cellular respiration.^[3]

NADP⁺ differs from NAD⁺ by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety. This extra phosphate is added by NAD⁺ kinase and removed by NADP⁺ phosphatase.^[4]

^ "NADP nicotinamide-adenine-dinucleotide phosphate". PubChem. U.S. National Library of Medicine. Archived from the original on November 17, 2020. Retrieved 2024-08-22.
^ Karlson P (2014-05-12). Introduction to Modern Biochemistry. Academic Press. ISBN 978-1-4832-6778-4.
^ Spaans SK, Weusthuis RA, van der Oost J, Kengen SW (2015). "NADPH-generating systems in bacteria and archaea". Frontiers in Microbiology. 6: 742. doi:10.3389/fmicb.2015.00742. PMC 4518329. PMID 26284036.
^ Kawai S, Murata K (April 2008). "Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)". Bioscience, Biotechnology, and Biochemistry. 72 (4): 919–930. doi:10.1271/bbb.70738. PMID 18391451.

[1] "NADP nicotinamide-adenine-dinucleotide phosphate". PubChem. U.S. National Library of Medicine. Archived from the original on November 17, 2020. Retrieved 2024-08-22.

[2] Karlson P (2014-05-12). Introduction to Modern Biochemistry. Academic Press. ISBN 978-1-4832-6778-4.

[pmid26284036-3] Spaans SK, Weusthuis RA, van der Oost J, Kengen SW (2015). "NADPH-generating systems in bacteria and archaea". Frontiers in Microbiology. 6: 742. doi:10.3389/fmicb.2015.00742. PMC 4518329. PMID 26284036.

[4] Kawai S, Murata K (April 2008). "Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)". Bioscience, Biotechnology, and Biochemistry. 72 (4): 919–930. doi:10.1271/bbb.70738. PMID 18391451.

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