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Chemical Compound Review

adpribose     [5-(6-aminopurin-9-yl)-3,4- dihydroxy...

Synonyms: AdoPPRib, ADP-Rib, ADP-ribose, ADP-D-ribose, HMDB01178, ...
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Disease relevance of adenosine diphosphate ribose

  • Exoenzyme S (ExoS), which has been implicated as a virulence factor of Pseudomonas aeruginosa, catalyzes transfer of the ADP-ribose moiety of NAD+ to many eukaryotic cellular proteins [1].
  • Studies of the mechanism of this effect show that a major alteration of poly(ADP-ribose) metabolism caused by hyperthermia involves a decrease in the rate of turnover of polymers of ADP-ribose [2].
  • These results suggested that a larger amount of monomers and short oligomers of ADP-ribose was synthesized in adenomatous polyps, while a smaller number of longer polymers was produced in cancers as compared with normal mucosa [3].
  • To determine the amino acid that served as the ADP-ribose acceptor, radiolabel from [adenine-U-14C]NAD was incorporated, in the presence of pertussis toxin, into the alpha subunit of transducin (0.3 mol/mol) [4].
  • Activation of Ca(2+)-dependent currents in cultured rat dorsal root ganglion neurones by a sperm factor and cyclic ADP-ribose [5].

High impact information on adenosine diphosphate ribose


Chemical compound and disease context of adenosine diphosphate ribose


Biological context of adenosine diphosphate ribose


Anatomical context of adenosine diphosphate ribose


Associations of adenosine diphosphate ribose with other chemical compounds


Gene context of adenosine diphosphate ribose

  • ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology [28].
  • The multifunctional ADP-ribosyl cyclase, CD38, catalyzes the cyclization of NAD(+) to cyclic ADP-ribose (cADPr) [29].
  • The hydrolysis of poly(ADP-ribose) by poly(ADP-ribose) glycohydrolase (PARG) was also required, since specific PARG inhibitors, which limit the production of ADP-ribose molecules, restored the function of ABC transporters [30].
  • We have recently characterized the protein product of the human NUDT9 gene as a highly specific ADP-ribose (ADPR) pyrophosphatase [31].
  • The role of NUDT5 in maintaining levels of free ADP-ribose in cells is discussed [32].

Analytical, diagnostic and therapeutic context of adenosine diphosphate ribose

  • Analysis of the reaction product by paper chromatography and Dowex 1 column chromatography indicated that the split product contained the ADP-ribose moiety but was not exactly identical with ADP-ribose [33].
  • Based on crystallography of the bacterial toxins, these regions are believed to form, in part, the catalytic site consistent with a common mechanism for the ADP-ribose transfer reaction [34].
  • Since this enzyme, which transfers ADP-ribose units to chromatin proteins, is known to activate DNA ligase, we attempted to determine whether ligation of one or both types of DNA break is required for monocytic differentiation [35].
  • To investigate this, we used highly purified recombinant ART2 and demonstrated that ART2 catalyzes the formation of an ADP-ribose polymer by sequencing gel and by HPLC and MS/MS mass spectrometry identification of PR-AMP, a breakdown product specific to poly(ADP-ribose) [36].
  • The active metabolite was purified by an identical high pressure liquid chromatography (HPLC) procedure used for cyclic ADP-ribose [37].


  1. The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. Fu, H., Coburn, J., Collier, R.J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  2. Mechanism of alteration of poly(adenosine diphosphate-ribose) metabolism by hyperthermia. Jonsson, G.G., Jacobson, E.L., Jacobson, M.K. Cancer Res. (1988) [Pubmed]
  3. Aberration of poly(adenosine diphosphate-ribose) metabolism in human colon adenomatous polyps and cancers. Hirai, K., Ueda, K., Hayaishi, O. Cancer Res. (1983) [Pubmed]
  4. Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. West, R.E., Moss, J., Vaughan, M., Liu, T., Liu, T.Y. J. Biol. Chem. (1985) [Pubmed]
  5. Activation of Ca(2+)-dependent currents in cultured rat dorsal root ganglion neurones by a sperm factor and cyclic ADP-ribose. Currie, K.P., Swann, K., Galione, A., Scott, R.H. Mol. Biol. Cell (1992) [Pubmed]
  6. Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in gram-positive bacteria. Madden, J.C., Ruiz, N., Caparon, M. Cell (2001) [Pubmed]
  7. Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability. d'Adda di Fagagna, F., Hande, M.P., Tong, W.M., Lansdorp, P.M., Wang, Z.Q., Jackson, S.P. Nat. Genet. (1999) [Pubmed]
  8. Inositol trisphosphate and cyclic ADP-ribose-mediated release of Ca2+ from single isolated pancreatic zymogen granules. Gerasimenko, O.V., Gerasimenko, J.V., Belan, P.V., Petersen, O.H. Cell (1996) [Pubmed]
  9. ATP-dependent accumulation and inositol trisphosphate- or cyclic ADP-ribose-mediated release of Ca2+ from the nuclear envelope. Gerasimenko, O.V., Gerasimenko, J.V., Tepikin, A.V., Petersen, O.H. Cell (1995) [Pubmed]
  10. Endogenous polymers of ADP-ribose are associated with the nuclear matrix. Cardenas-Corona, M.E., Jacobson, E.L., Jacobson, M.K. J. Biol. Chem. (1987) [Pubmed]
  11. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Gabelli, S.B., Bianchet, M.A., Ohnishi, Y., Ichikawa, Y., Bessman, M.J., Amzel, L.M. Biochemistry (2002) [Pubmed]
  12. Cyclic ADP-ribose is a second messenger in the lipopolysaccharide-stimulated activation of murine N9 microglial cell line. Franco, L., Bodrato, N., Moreschi, I., Usai, C., Bruzzone, S., Scarf I, S., Zocchi, E., De Flora, A. J. Neurochem. (2006) [Pubmed]
  13. Amino acid-specific ADP-ribosylation: structural characterization and chemical differentiation of ADP-ribose-cysteine adducts formed nonenzymatically and in a pertussis toxin-catalyzed reaction. McDonald, L.J., Wainschel, L.A., Oppenheimer, N.J., Moss, J. Biochemistry (1992) [Pubmed]
  14. Immunochemical detection of guanine nucleotide binding proteins mono-ADP-ribosylated by bacterial toxins. Eide, B., Gierschik, P., Spiegel, A. Biochemistry (1986) [Pubmed]
  15. Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo. Partida-Sánchez, S., Cockayne, D.A., Monard, S., Jacobson, E.L., Oppenheimer, N., Garvy, B., Kusser, K., Goodrich, S., Howard, M., Harmsen, A., Randall, T.D., Lund, F.E. Nat. Med. (2001) [Pubmed]
  16. Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity. Zhang, J., Dawson, V.L., Dawson, T.M., Snyder, S.H. Science (1994) [Pubmed]
  17. Ligation of CD38 suppresses human B lymphopoiesis. Kumagai, M., Coustan-Smith, E., Murray, D.J., Silvennoinen, O., Murti, K.G., Evans, W.E., Malavasi, F., Campana, D. J. Exp. Med. (1995) [Pubmed]
  18. Discovering new ADP-ribose polymer cycles: protecting the genome and more. Jacobson, M.K., Jacobson, E.L. Trends Biochem. Sci. (1999) [Pubmed]
  19. The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase. Kickhoefer, V.A., Siva, A.C., Kedersha, N.L., Inman, E.M., Ruland, C., Streuli, M., Rome, L.H. J. Cell Biol. (1999) [Pubmed]
  20. Regulation of calcium signalling in T lymphocytes by the second messenger cyclic ADP-ribose. Guse, A.H., da Silva, C.P., Berg, I., Skapenko, A.L., Weber, K., Heyer, P., Hohenegger, M., Ashamu, G.A., Schulze-Koops, H., Potter, B.V., Mayr, G.W. Nature (1999) [Pubmed]
  21. Cyclic ADP-ribose in insulin secretion from pancreatic beta cells. Takasawa, S., Nata, K., Yonekura, H., Okamoto, H. Science (1993) [Pubmed]
  22. Release of Ca2+ from individual plant vacuoles by both InsP3 and cyclic ADP-ribose. Allen, G.J., Muir, S.R., Sanders, D. Science (1995) [Pubmed]
  23. Unusual levels of (ADP-ribose)n and DNA synthesis in ataxia telangiectasia cells following gamma-ray irradiation. Edwards, M.J., Taylor, A.M. Nature (1980) [Pubmed]
  24. All-trans-retinoic acid stimulates synthesis of cyclic ADP-ribose in renal LLC-PK1 cells. Beers, K.W., Chini, E.N., Dousa, T.P. J. Clin. Invest. (1995) [Pubmed]
  25. Two different but converging messenger pathways to intracellular Ca(2+) release: the roles of nicotinic acid adenine dinucleotide phosphate, cyclic ADP-ribose and inositol trisphosphate. Cancela, J.M., Gerasimenko, O.V., Gerasimenko, J.V., Tepikin, A.V., Petersen, O.H. EMBO J. (2000) [Pubmed]
  26. Regulation of glutamate dehydrogenase by reversible ADP-ribosylation in mitochondria. Herrero-Yraola, A., Bakhit, S.M., Franke, P., Weise, C., Schweiger, M., Jorcke, D., Ziegler, M. EMBO J. (2001) [Pubmed]
  27. Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Zhao, K., Harshaw, R., Chai, X., Marmorstein, R. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  28. ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. Perraud, A.L., Fleig, A., Dunn, C.A., Bagley, L.A., Launay, P., Schmitz, C., Stokes, A.J., Zhu, Q., Bessman, M.J., Penner, R., Kinet, J.P., Scharenberg, A.M. Nature (2001) [Pubmed]
  29. CD38/ADP-ribosyl cyclase: A new role in the regulation of osteoclastic bone resorption. Sun, L., Adebanjo, O.A., Moonga, B.S., Corisdeo, S., Anandatheerthavarada, H.K., Biswas, G., Arakawa, T., Hakeda, Y., Koval, A., Sodam, B., Bevis, P.J., Moser, A.J., Lai, F.A., Epstein, S., Troen, B.R., Kumegawa, M., Zaidi, M. J. Cell Biol. (1999) [Pubmed]
  30. UV irradiation inhibits ABC transporters via generation of ADP-ribose by concerted action of poly(ADP-ribose) polymerase-1 and glycohydrolase. Dumitriu, I.E., Voll, R.E., Kolowos, W., Gaipl, U.S., Heyder, P., Kalden, J.R., Herrmann, M. Cell Death Differ. (2004) [Pubmed]
  31. NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase. Perraud, A.L., Shen, B., Dunn, C.A., Rippe, K., Smith, M.K., Bessman, M.J., Stoddard, B.L., Scharenberg, A.M. J. Biol. Chem. (2003) [Pubmed]
  32. Cloning and characterization of a new member of the Nudix hydrolases from human and mouse. Yang, H., Slupska, M.M., Wei, Y.F., Tai, J.H., Luther, W.M., Xia, Y.R., Shih, D.M., Chiang, J.H., Baikalov, C., Fitz-Gibbon, S., Phan, I.T., Conrad, A., Miller, J.H. J. Biol. Chem. (2000) [Pubmed]
  33. Novel enzyme from rat liver that cleaves an ADP-ribosyl histone linkage. Okayama, H., Honda, M., Hayaishi, O. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  34. Molecular characterization of a glycosylphosphatidylinositol-linked ADP-ribosyltransferase from lymphocytes. Okazaki, I.J., Kim, H.J., McElvaney, N.G., Lesma, E., Moss, J. Blood (1996) [Pubmed]
  35. Contrasting patterns of DNA strand breakage and ADP-ribosylation-dependent DNA ligation during granulocyte and monocyte differentiation. Khan, Z., Francis, G.E. Blood (1987) [Pubmed]
  36. ART2, a T Cell Surface Mono-ADP-ribosyltransferase, Generates Extracellular Poly(ADP-ribose). Morrison, A.R., Moss, J., Stevens, L.A., Evans, J.E., Farrell, C., Merithew, E., Lambright, D.G., Greiner, D.L., Mordes, J.P., Rossini, A.A., Bortell, R. J. Biol. Chem. (2006) [Pubmed]
  37. Widespread occurrence in animal tissues of an enzyme catalyzing the conversion of NAD+ into a cyclic metabolite with intracellular Ca2+-mobilizing activity. Rusinko, N., Lee, H.C. J. Biol. Chem. (1989) [Pubmed]
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