Adenosine diphosphate ribose

Adenosine diphosphate ribose
Names
Other names
ADP ribose
ADPR
Adenosine 5'-diphosphoribose
Identifiers
3D model (JSmol)
ChEMBL
ChemSpider
MeSH Adenosine+Diphosphate+Ribose
UNII
  • InChI=1S/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(24)9(23)6(31-14)2-30-35(26,27)34-36(28,29)33-15-11(25)8(22)5(1-21)32-15/h3-6,8-11,14-15,21-25H,1-2H2,(H4,16,17,18,26,27,28,29)/p+1/t5-,6+,8-,9+,10+,11-,14+,15+/m0/s1 ☒N
    Key: YNCNQNWXUFCWJS-DKMYFHGXSA-O ☒N
  • InChI=1/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(24)9(23)6(31-14)2-30-35(26,27)34-36(28,29)33-15-11(25)8(22)5(1-21)32-15/h3-6,8-11,14-15,21-25H,1-2H2,(H4,16,17,18,26,27,28,29)/p+1/t5-,6+,8-,9+,10+,11-,14+,15+/m0/s1
    Key: YNCNQNWXUFCWJS-LKOYDKQFBH
  • O=P(O[C@H]1O[C@H]([C@H](O)[C@@H]1O)CO)(O)OP(=O)(OC[C@H]4O[C@@H](n3c2ncnc(N)c2nc3)[C@H](O)[C@@H]4O)O
Properties
C15H23N5O14P2
Molar mass 559.316 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Adenosine diphosphate ribose (ADPR) is an ester molecule formed into chains by the enzyme poly ADP ribose polymerase.[1] ADPR is created from cyclic ADP-ribose (cADPR) by the CD38 enzyme using nicotinamide adenine dinucleotide (NAD+) as a cofactor.[1]

ADPR binds to and activates the TRPM2 ion channel.[2] ADPR is the most potent agonist of the TRPM2 channel.[3] cADPR also binds to TPRM2, and the action of both molecules is synergistic, with both molecules enhancing the action of the other molecule in activating the TRPM2 channel.[4] Researchers are not sure how the Adenosine diphosphate reacts with the TRPM2 channel, but the ribose sugar may play a role in activating the TRPM2 ion channel.[5]

See also

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References

[edit]
  1. ^ a b Braidy N, Berg J, Clement J, Sachdev P (2019). "Role of Nicotinamide Adenine Dinucleotide and Related Precursors as Therapeutic Targets for Age-Related Degenerative Diseases: Rationale, Biochemistry, Pharmacokinetics, and Outcomes". Antioxidants & Redox Signaling. 10 (2): 251–294. doi:10.1089/ars.2017.7269. PMC 6277084. PMID 29634344.
  2. ^ Fonfria E, Marshall IC, Benham CD, et al. (September 2004). "TRPM2 channel opening in response to oxidative stress is dependent on activation of poly(ADP-ribose) polymerase". Br. J. Pharmacol. 143 (1): 186–92. doi:10.1038/sj.bjp.0705914. PMC 1575275. PMID 15302683.
  3. ^ Yu P, Cai X, Liang Y, Yang W (2019). "Roles of NAD + and Its Metabolites Regulated Calcium Channels in Cancer". Molecules. 25 (20): 4826. doi:10.3390/molecules25204826. PMC 7587972. PMID 33092205.
  4. ^ Lee HC (2011). "Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling". Science China Life Sciences. 54 (8): 699–711. doi:10.1007/s11427-011-4197-3. PMID 21786193. S2CID 24286381.
  5. ^ Baszczyňski, Ondřej; Watt, Joanna M.; Rozewitz, Monika D.; Guse, Andreas H.; Fliegert, Ralf; Potter, Barry V. L. (2019). "Synthesis of Terminal Ribose Analogues of Adenosine 5′-Diphosphate Ribose as Probes for the Transient Receptor Potential Cation Channel TRPM2". The Journal of Organic Chemistry. 84 (10): 6143–6157. doi:10.1021/acs.joc.9b00338. PMC 6528165. PMID 30978018.


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