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Nicotinamide adenine dinucleotide phosphate

October 19, 2023

Not to be confused with Nicotinamide adenine dinucleotide (NAD+/NADH).

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ 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 of NADP+, the oxidized form. NADP+ is used by all forms of cellular life.[1]

Nicotinamide adenine dinucleotide phosphate
Identifiers
  • 53-59-8 Y
3D model (JSmol)
  • Interactive image
ChEBI
  • CHEBI:44409 Y
ChEMBL
  • ChEMBL2364573 N
ChemSpider
  • 5674 Y
ECHA InfoCard 100.000.163
MeSH NADP
  • 5885
UNII
  • BY8P107XEP Y
  • 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 Y
    Key: XJLXINKUBYWONI-NNYOXOHSSA-N Y
  • 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
  • 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
C21H29N7O17P3
Molar mass 744.416 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
N verify (what is YN ?)

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.[2]

Biosynthesis Edit

NADP+ Edit

In general, NADP+ is synthesized before NADPH is. Such a reaction usually starts with NAD+ from either the de-novo or the salvage pathway, with NAD+ kinase adding the extra phosphate group. ADP-ribosyl cyclase allows for synthesis from nicotinamide in the salvage pathway, and NADP+ phosphatase can convert NADPH back to NADH to maintain a balance.[1] Some forms of the NAD+ kinase, notably the one in mitochondria, can also accept NADH to turn it directly into NADPH.[3][4] The prokaryotic pathway is less well understood, but with all the similar proteins the process should work in a similar way.[1]

NADPH Edit

NADPH is produced from NADP+. The major source of NADPH in animals and other non-photosynthetic organisms is the pentose phosphate pathway, by glucose-6-phosphate dehydrogenase (G6PDH) in the first step. The pentose phosphate pathway also produces pentose, another important part of NAD(P)H, from glucose. Some bacteria also use G6PDH for the Entner–Doudoroff pathway, but NADPH production remains the same.[1]

Ferredoxin–NADP+ reductase, present in all domains of life, is a major source of NADPH in photosynthetic organisms including plants and cyanobacteria. It appears in the last step of the electron chain of the light reactions of photosynthesis. It is used as reducing power for the biosynthetic reactions in the Calvin cycle to assimilate carbon dioxide and help turn the carbon dioxide into glucose. It has functions in accepting electrons in other non-photosynthetic pathways as well: it is needed in the reduction of nitrate into ammonia for plant assimilation in nitrogen cycle and in the production of oils.[1]

There are several other lesser-known mechanisms of generating NADPH, all of which depend on the presence of mitochondria in eukaryotes. The key enzymes in these carbon-metabolism-related processes are NADP-linked isoforms of malic enzyme, isocitrate dehydrogenase (IDH), and glutamate dehydrogenase. In these reactions, NADP+ acts like NAD+ in other enzymes as an oxidizing agent.[5] The isocitrate dehydrogenase mechanism appears to be the major source of NADPH in fat and possibly also liver cells.[6] These processes are also found in bacteria. Bacteria can also use a NADP-dependent glyceraldehyde 3-phosphate dehydrogenase for the same purpose. Like the pentose phosphate pathway, these pathways are related to parts of glycolysis.[1] Another carbon metabolism-related pathway involved in the generation of NADPH is the mitochondrial folate cycle, which uses principally serine as a source of one-carbon units to sustain nucleotide synthesis and redox homeostasis in mitochondria. Mitochondrial folate cycle has been recently suggested as the principal contributor to NADPH generation in mitochondria of cancer cells.[7]

NADPH can also be generated through pathways unrelated to carbon metabolism. The ferredoxin reductase is such an example. Nicotinamide nucleotide transhydrogenase transfers the hydrogen between NAD(P)H and NAD(P)+, and is found in eukaryotic mitochondria and many bacteria. There are versions that depend on a proton gradient to work and ones that do not. Some anaerobic organisms use NADP+-linked hydrogenase, ripping a hydride from hydrogen gas to produce a proton and NADPH.[1]

Like NADH, NADPH is fluorescent. NADPH in aqueous solution excited at the nicotinamide absorbance of ~335 nm (near UV) has a fluorescence emission which peaks at 445-460 nm (violet to blue). NADP+ has no appreciable fluorescence.[8]

Function Edit

NADPH provides the reducing equivalents, usually hydrogen atoms, for biosynthetic reactions and the oxidation-reduction involved in protecting against the toxicity of reactive oxygen species (ROS), allowing the regeneration of glutathione (GSH).[9] NADPH is also used for anabolic pathways, such as cholesterol synthesis, steroid synthesis,[10] ascorbic acid synthesis,[10] xylitol synthesis,[10] cytosolic fatty acid synthesis[10] and microsomal fatty acid chain elongation.

The NADPH system is also responsible for generating free radicals in immune cells by NADPH oxidase. These radicals are used to destroy pathogens in a process termed the respiratory burst.[11] It is the source of reducing equivalents for cytochrome P450 hydroxylation of aromatic compounds, steroids, alcohols, and drugs.

Stability Edit

NADH and NADPH are very stable in basic solutions, but NAD+ and NADP+ are degraded in basic solutions into a fluorescent product that can be used conveniently for quantitation. Conversely, NADPH and NADH are degraded by acidic solutions while NAD+/NADP+ are fairly stable to acid.[12]

Enzymes that use NADP(H) as a coenzyme Edit

  • Adrenodoxin reductase: This enzyme is present ubiquitously in most organisms.[13] It transfers two electrons from NADPH to FAD. In vertebrates, it serves as the first enzyme in the chain of mitochondrial P450 systems that synthesize steroid hormones.[14]

Enzymes that use NADP(H) as a substrate Edit

In 2018 and 2019, the first two reports of enzymes that catalyze the removal of the 2' phosphate of NADP(H) in eukaryotes emerged. First the cytoplasmic protein MESH1 (Q8N4P3),[15] then the mitochondrial protein nocturnin[16][17] were reported. Of note, the structures and NADPH binding of MESH1 (5VXA) and nocturnin (6NF0) are not related.

Ball-and-stick models of NADP+ and NADPH
  •  

    NADP+

  •  

    NADPH

References Edit

  1. ^ a b c d e f g 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.
  2. ^ 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): 919–30. doi:10.1271/bbb.70738. PMID 18391451.
  3. ^ Iwahashi Y, Hitoshio A, Tajima N, Nakamura T (April 1989). "Characterization of NADH kinase from Saccharomyces cerevisiae". Journal of Biochemistry. 105 (4): 588–93. doi:10.1093/oxfordjournals.jbchem.a122709. PMID 2547755.
  4. ^ Iwahashi Y, Nakamura T (June 1989). "Localization of the NADH kinase in the inner membrane of yeast mitochondria". Journal of Biochemistry. 105 (6): 916–21. doi:10.1093/oxfordjournals.jbchem.a122779. PMID 2549021.
  5. ^ Hanukoglu I, Rapoport R (Feb–May 1995). "Routes and regulation of NADPH production in steroidogenic mitochondria". Endocrine Research. 21 (1–2): 231–41. doi:10.3109/07435809509030439. PMID 7588385.
  6. ^ Palmer, Michael. . Metabolism Course Notes. Archived from the original on 6 June 2013. Retrieved 6 April 2012.
  7. ^ Ciccarese, F.; Ciminale, V. (June 2017). "Escaping Death: Mitochondrial Redox Homeostasis in Cancer Cells". Front Oncol. 7: 117. doi:10.3389/fonc.2017.00117. PMC 5465272. PMID 28649560.
  8. ^ Blacker, Thomas S.; Mann, Zoe F.; Gale, Jonathan E.; Ziegler, Mathias; Bain, Angus J.; Szabadkai, Gyorgy; Duchen, Michael R. (2014-05-29). "Separating NADH and NADPH fluorescence in live cells and tissues using FLIM". Nature Communications. Springer Science and Business Media LLC. 5 (1): 3936. Bibcode:2014NatCo...5.3936B. doi:10.1038/ncomms4936. ISSN 2041-1723. PMC 4046109. PMID 24874098.
  9. ^ Rush GF, Gorski JR, Ripple MG, Sowinski J, Bugelski P, Hewitt WR (May 1985). "Organic hydroperoxide-induced lipid peroxidation and cell death in isolated hepatocytes". Toxicology and Applied Pharmacology. 78 (3): 473–83. doi:10.1016/0041-008X(85)90255-8. PMID 4049396.
  10. ^ a b c d Rodwell, Victor (2015). Harper's illustrated Biochemistry, 30th edition. USA: McGraw Hill. pp. 123–124, 166, 200–201. ISBN 978-0-07-182537-5.
  11. ^ Ogawa K, Suzuki K, Okutsu M, Yamazaki K, Shinkai S (October 2008). "The association of elevated reactive oxygen species levels from neutrophils with low-grade inflammation in the elderly". Immunity & Ageing. 5: 13. doi:10.1186/1742-4933-5-13. PMC 2582223. PMID 18950479.
  12. ^ Passonneau, Janet (1993). Enzymatic analysis : a practical guide. Totowa, NJ: Humana Press. p. 3,10. ISBN 978-0-89603-238-5. OCLC 26397387.
  13. ^ Hanukoglu I (December 2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme". Journal of Molecular Evolution. 85 (5–6): 205–218. Bibcode:2017JMolE..85..205H. doi:10.1007/s00239-017-9821-9. PMID 29177972. S2CID 7120148.
  14. ^ Hanukoglu I (December 1992). "Steroidogenic enzymes: structure, function, and role in regulation of steroid hormone biosynthesis". The Journal of Steroid Biochemistry and Molecular Biology. 43 (8): 779–804. doi:10.1016/0960-0760(92)90307-5. PMID 22217824. S2CID 112729.
  15. ^ Ding CKC, Rose J, Wu J, Sun T, Chen KY, Chen PH, Xu E, Tian S, Akinwuntan J, Guan Z, Zhou P, Chi JTA (2018). "Mammalian stringent-like response mediated by the cytosolic NADPH phosphatase MESH1". bioRxiv. doi:10.1101/325266.
  16. ^ Estrella MA, Du J, Chen L, Rath S, Prangley E, Chitrakar A, Aoki T, Schedl P, Rabinowitz J, Korennykh A (2019). "The Metabolites NADP+ and NADPH are the Targets of the Circadian Protein Nocturnin (Curled)". bioRxiv. 10 (1): 2367. doi:10.1101/534560. PMC 6542800. PMID 31147539.
  17. ^ Estrella MA, Du J, Chen L, Rath S, Prangley E, Chitrakar A, et al. (May 2019). "+ and NADPH are the targets of the circadian protein Nocturnin (Curled)". Nature Communications. 10 (1): 2367. doi:10.1038/s41467-019-10125-z. PMC 6542800. PMID 31147539.

October 19, 2023
nicotinamide, adenine, dinucleotide, phosphate, confused, with, nicotinamide, adenine, dinucleotide, nadh, abbreviated, nadp, older, notation, triphosphopyridine, nucleotide, cofactor, used, anabolic, reactions, such, calvin, cycle, lipid, nucleic, acid, synth. Not to be confused with Nicotinamide adenine dinucleotide NAD NADH Nicotinamide adenine dinucleotide phosphate abbreviated NADP 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 of NADP the oxidized form NADP is used by all forms of cellular life 1 Nicotinamide adenine dinucleotide phosphate IdentifiersCAS Number 53 59 8 Y3D model JSmol Interactive imageChEBI CHEBI 44409 YChEMBL ChEMBL2364573 NChemSpider 5674 YECHA InfoCard 100 000 163MeSH NADPPubChem CID 5885UNII BY8P107XEP YInChI 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 YKey XJLXINKUBYWONI NNYOXOHSSA N YInChI 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 s1Key XJLXINKUBYWONI NNYOXOHSBNSMILES 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 OPropertiesChemical formula C 21H 29N 7O 17P 3Molar mass 744 416 g mol 1Except where otherwise noted data are given for materials in their standard state at 25 C 77 F 100 kPa N verify what is Y N Infobox references 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 2 Contents 1 Biosynthesis 1 1 NADP 1 2 NADPH 2 Function 3 Stability 4 Enzymes that use NADP H as a coenzyme 5 Enzymes that use NADP H as a substrate 6 ReferencesBiosynthesis EditNADP Edit In general NADP is synthesized before NADPH is Such a reaction usually starts with NAD from either the de novo or the salvage pathway with NAD kinase adding the extra phosphate group ADP ribosyl cyclase allows for synthesis from nicotinamide in the salvage pathway and NADP phosphatase can convert NADPH back to NADH to maintain a balance 1 Some forms of the NAD kinase notably the one in mitochondria can also accept NADH to turn it directly into NADPH 3 4 The prokaryotic pathway is less well understood but with all the similar proteins the process should work in a similar way 1 NADPH Edit NADPH is produced from NADP The major source of NADPH in animals and other non photosynthetic organisms is the pentose phosphate pathway by glucose 6 phosphate dehydrogenase G6PDH in the first step The pentose phosphate pathway also produces pentose another important part of NAD P H from glucose Some bacteria also use G6PDH for the Entner Doudoroff pathway but NADPH production remains the same 1 Ferredoxin NADP reductase present in all domains of life is a major source of NADPH in photosynthetic organisms including plants and cyanobacteria It appears in the last step of the electron chain of the light reactions of photosynthesis It is used as reducing power for the biosynthetic reactions in the Calvin cycle to assimilate carbon dioxide and help turn the carbon dioxide into glucose It has functions in accepting electrons in other non photosynthetic pathways as well it is needed in the reduction of nitrate into ammonia for plant assimilation in nitrogen cycle and in the production of oils 1 There are several other lesser known mechanisms of generating NADPH all of which depend on the presence of mitochondria in eukaryotes The key enzymes in these carbon metabolism related processes are NADP linked isoforms of malic enzyme isocitrate dehydrogenase IDH and glutamate dehydrogenase In these reactions NADP acts like NAD in other enzymes as an oxidizing agent 5 The isocitrate dehydrogenase mechanism appears to be the major source of NADPH in fat and possibly also liver cells 6 These processes are also found in bacteria Bacteria can also use a NADP dependent glyceraldehyde 3 phosphate dehydrogenase for the same purpose Like the pentose phosphate pathway these pathways are related to parts of glycolysis 1 Another carbon metabolism related pathway involved in the generation of NADPH is the mitochondrial folate cycle which uses principally serine as a source of one carbon units to sustain nucleotide synthesis and redox homeostasis in mitochondria Mitochondrial folate cycle has been recently suggested as the principal contributor to NADPH generation in mitochondria of cancer cells 7 NADPH can also be generated through pathways unrelated to carbon metabolism The ferredoxin reductase is such an example Nicotinamide nucleotide transhydrogenase transfers the hydrogen between NAD P H and NAD P and is found in eukaryotic mitochondria and many bacteria There are versions that depend on a proton gradient to work and ones that do not Some anaerobic organisms use NADP linked hydrogenase ripping a hydride from hydrogen gas to produce a proton and NADPH 1 Like NADH NADPH is fluorescent NADPH in aqueous solution excited at the nicotinamide absorbance of 335 nm near UV has a fluorescence emission which peaks at 445 460 nm violet to blue NADP has no appreciable fluorescence 8 Function EditNADPH provides the reducing equivalents usually hydrogen atoms for biosynthetic reactions and the oxidation reduction involved in protecting against the toxicity of reactive oxygen species ROS allowing the regeneration of glutathione GSH 9 NADPH is also used for anabolic pathways such as cholesterol synthesis steroid synthesis 10 ascorbic acid synthesis 10 xylitol synthesis 10 cytosolic fatty acid synthesis 10 and microsomal fatty acid chain elongation The NADPH system is also responsible for generating free radicals in immune cells by NADPH oxidase These radicals are used to destroy pathogens in a process termed the respiratory burst 11 It is the source of reducing equivalents for cytochrome P450 hydroxylation of aromatic compounds steroids alcohols and drugs Stability EditNADH and NADPH are very stable in basic solutions but NAD and NADP are degraded in basic solutions into a fluorescent product that can be used conveniently for quantitation Conversely NADPH and NADH are degraded by acidic solutions while NAD NADP are fairly stable to acid 12 Enzymes that use NADP H as a coenzyme EditAdrenodoxin reductase This enzyme is present ubiquitously in most organisms 13 It transfers two electrons from NADPH to FAD In vertebrates it serves as the first enzyme in the chain of mitochondrial P450 systems that synthesize steroid hormones 14 Enzymes that use NADP H as a substrate EditIn 2018 and 2019 the first two reports of enzymes that catalyze the removal of the 2 phosphate of NADP H in eukaryotes emerged First the cytoplasmic protein MESH1 Q8N4P3 15 then the mitochondrial protein nocturnin 16 17 were reported Of note the structures and NADPH binding of MESH1 5VXA and nocturnin 6NF0 are not related Ball and stick models of NADP and NADPH nbsp NADP nbsp NADPHReferences Edit a b c d e f g 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 30 doi 10 1271 bbb 70738 PMID 18391451 Iwahashi Y Hitoshio A Tajima N Nakamura T April 1989 Characterization of NADH kinase from Saccharomyces cerevisiae Journal of Biochemistry 105 4 588 93 doi 10 1093 oxfordjournals jbchem a122709 PMID 2547755 Iwahashi Y Nakamura T June 1989 Localization of the NADH kinase in the inner membrane of yeast mitochondria Journal of Biochemistry 105 6 916 21 doi 10 1093 oxfordjournals jbchem a122779 PMID 2549021 Hanukoglu I Rapoport R Feb May 1995 Routes and regulation of NADPH production in steroidogenic mitochondria Endocrine Research 21 1 2 231 41 doi 10 3109 07435809509030439 PMID 7588385 Palmer Michael 10 4 3 Supply of NADPH for fatty acid synthesis Metabolism Course Notes Archived from the original on 6 June 2013 Retrieved 6 April 2012 Ciccarese F Ciminale V June 2017 Escaping Death Mitochondrial Redox Homeostasis in Cancer Cells Front Oncol 7 117 doi 10 3389 fonc 2017 00117 PMC 5465272 PMID 28649560 Blacker Thomas S Mann Zoe F Gale Jonathan E Ziegler Mathias Bain Angus J Szabadkai Gyorgy Duchen Michael R 2014 05 29 Separating NADH and NADPH fluorescence in live cells and tissues using FLIM Nature Communications Springer Science and Business Media LLC 5 1 3936 Bibcode 2014NatCo 5 3936B doi 10 1038 ncomms4936 ISSN 2041 1723 PMC 4046109 PMID 24874098 Rush GF Gorski JR Ripple MG Sowinski J Bugelski P Hewitt WR May 1985 Organic hydroperoxide induced lipid peroxidation and cell death in isolated hepatocytes Toxicology and Applied Pharmacology 78 3 473 83 doi 10 1016 0041 008X 85 90255 8 PMID 4049396 a b c d Rodwell Victor 2015 Harper s illustrated Biochemistry 30th edition USA McGraw Hill pp 123 124 166 200 201 ISBN 978 0 07 182537 5 Ogawa K Suzuki K Okutsu M Yamazaki K Shinkai S October 2008 The association of elevated reactive oxygen species levels from neutrophils with low grade inflammation in the elderly Immunity amp Ageing 5 13 doi 10 1186 1742 4933 5 13 PMC 2582223 PMID 18950479 Passonneau Janet 1993 Enzymatic analysis a practical guide Totowa NJ Humana Press p 3 10 ISBN 978 0 89603 238 5 OCLC 26397387 Hanukoglu I December 2017 Conservation of the Enzyme Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase A Ubiquitous Enzyme Journal of Molecular Evolution 85 5 6 205 218 Bibcode 2017JMolE 85 205H doi 10 1007 s00239 017 9821 9 PMID 29177972 S2CID 7120148 Hanukoglu I December 1992 Steroidogenic enzymes structure function and role in regulation of steroid hormone biosynthesis The Journal of Steroid Biochemistry and Molecular Biology 43 8 779 804 doi 10 1016 0960 0760 92 90307 5 PMID 22217824 S2CID 112729 Ding CKC Rose J Wu J Sun T Chen KY Chen PH Xu E Tian S Akinwuntan J Guan Z Zhou P Chi JTA 2018 Mammalian stringent like response mediated by the cytosolic NADPH phosphatase MESH1 bioRxiv doi 10 1101 325266 Estrella MA Du J Chen L Rath S Prangley E Chitrakar A Aoki T Schedl P Rabinowitz J Korennykh A 2019 The Metabolites NADP and NADPH are the Targets of the Circadian Protein Nocturnin Curled bioRxiv 10 1 2367 doi 10 1101 534560 PMC 6542800 PMID 31147539 Estrella MA Du J Chen L Rath S Prangley E Chitrakar A et al May 2019 and NADPH are the targets of the circadian protein Nocturnin Curled Nature Communications 10 1 2367 doi 10 1038 s41467 019 10125 z PMC 6542800 PMID 31147539 Retrieved from https en wikipedia org w index php title Nicotinamide adenine dinucleotide phosphate amp oldid 1180770101, wikipedia, wiki, book, books, library,

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