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Chemical Compound Review

ADPG     [[(2R,3S,4R,5R)-5-(6- aminopurin-9-yl)-3,4...

Synonyms: ADP-glucose, ADP Glucose, CHEMBL227552, CHEBI:15751, HMDB06557, ...
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Disease relevance of ADP Glucose


High impact information on ADP Glucose

  • The main regulatory step takes place at the level of ADP-glucose synthesis, a reaction catalyzed by ADP-Glc pyrophosphorylase (PPase) [6].
  • A complete rice NPP cDNA, designated as NPP1, was isolated, characterized, and overexpressed in transgenic plants displaying high ADPG hydrolytic activity [7].
  • These observations provide direct evidence that Sh2 encodes a subunit for endosperm ADP-glucose pyrophosphorylase [8].
  • Although the cloning and identification were done independently of any knowledge concerning the product of this gene, examination of the deduced amino acid sequence revealed much similarity to known ADP-glucose pyrophosphorylase subunits of plants and bacteria, including regions involved in substrate binding and activator binding [8].
  • A proteomics approach in combination with affinity chromatography and a fluorescent thiol probe led to the identification of 42 potential Trx target proteins, 13 not previously recognized, including a major membrane transporter (Brittle-1 or ADP-glucose transporter) [9].

Chemical compound and disease context of ADP Glucose


Biological context of ADP Glucose

  • The generation of these revertant enzymes provides additional structure-function information on the allosteric regulation of higher plant ADP-glucose pyrophosphorylases and validates a strategy for developing novel variants of the enzyme that may be useful in manipulating starch biosynthesis in higher plants [14].
  • Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation [15].
  • Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics [14].
  • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C gene [16].
  • These results suggest that the 2 glycyl residues in the conserved Lys-X-Gly-Gly sequence, in particular the one closer to the ADP-glucose-binding lysyl residue, participate in catalysis by assisting conformational change(s) of the active site or stabilizing the transition state [17].

Anatomical context of ADP Glucose

  • The overall results show that, essentially similar to cereal endosperms, most of the ADPG linked to starch biosynthesis in source leaves occurs in the cytosol [18].
  • Membranes of the wild-type S. meliloti strain 2011 catalyze the glycosylation of Kdo(2)-[4'-(32)P]lipid IV(A) at comparable rates using a diverse set of sugar nucleotides, including GDP-mannose, ADP-mannose, UDP-glucose, and ADP-glucose [19].
  • ADP-glucose pyrophosphorylase is located in the plastid in developing tomato fruit [20].
  • Starch synthase, ADP-glucose pyrophosphorylase and each of the glycolytic enzymes showed appreciable latency when assayed in unfractionated lysates of protoplasts [21].
  • Structurally intact and metabolically competent mitochondria isolated from liquid-culture cells of sycamore (Acer pseudoplatanus L.) were shown to incorporate ADPglucose [22].

Associations of ADP Glucose with other chemical compounds

  • This evidence is consistent with the idea that synthesis of the ADPG linked to starch biosynthesis takes place in the cytosol by means of sucrose synthase, whereas AGP channels the glucose units derived from the starch breakdown [18].
  • Kinetic studies with ADP-glucose synthase show that 1,6-hexanediol bisphosphate (1,6-hexanediol-P2) is an effective activator that causes the enzyme to have a higher apparent affinity for ATP- and ADP-glucose than when fructose-1,6-P2 is the activator [23].
  • We recently discovered that post-translational redox modulation of ADP-glucose pyrophosphorylase (AGPase) is a powerful new mechanism to adjust the rate of starch synthesis to the availability of sucrose in growing potato tubers [24].
  • The solution conformations of UDPG, UDPGN, UDPGal, UDPM, UDPGluc, UDPGalc, ADPG, ADPM, GDPG, GDPM, and CDPG and their components Glu-1-P, Gal-1-P, Man-1-P, Gluc-1-P, Galc-1-P, ADP, GDP, UDP, and CDP are studied by high resolution fast Fourier transform nuclear magnetic resonance spectroscopy with iterative computer line shape simulation [25].
  • This microorganism synthesizes trehalose through two major pathways, OtsBA and TreYZ, by using UDP-glucose and ADP-glucose, respectively, as the glucosyl donors [26].

Gene context of ADP Glucose


Analytical, diagnostic and therapeutic context of ADP Glucose


  1. Identification of UDP-glucose as an intermediate in the biosynthesis of the membrane-derived oligosaccharides of Escherichia coli. Schulman, H., Kennedy, E.P. J. Biol. Chem. (1977) [Pubmed]
  2. Structure-function relationships of cyanobacterial ADP-glucose pyrophosphorylase. Site-directed mutagenesis and chemical modification of the activator-binding sites of ADP-glucose pyrophosphorylase from Anabaena PCC 7120. Charng, Y.Y., Iglesias, A.A., Preiss, J. J. Biol. Chem. (1994) [Pubmed]
  3. Comparison of the 5' flanking regions of the Salmonella typhimurium and Escherichia coli glgC genes, encoding ADP glucose pyrophosphorylases. Romeo, T., Moore, J. Nucleic Acids Res. (1991) [Pubmed]
  4. Characterization of chimeric ADPglucose pyrophosphorylases of Escherichia coli and Agrobacterium tumefaciens. Importance of the C-terminus on the selectivity for allosteric regulators. Ballicora, M.A., Sesma, J.I., Iglesias, A.A., Preiss, J. Biochemistry (2002) [Pubmed]
  5. Purification and characterization of a thermostable ADP-glucose pyrophosphorylase from Thermus caldophilus GK-24. Ko, J.H., Kim, C.H., Lee, D.S., Kim, Y.S. Biochem. J. (1996) [Pubmed]
  6. ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Ballicora, M.A., Iglesias, A.A., Preiss, J. Microbiol. Mol. Biol. Rev. (2003) [Pubmed]
  7. Rice Plastidial N-Glycosylated Nucleotide Pyrophosphatase/Phosphodiesterase Is Transported from the ER-Golgi to the Chloroplast through the Secretory Pathway. Nanjo, Y., Oka, H., Ikarashi, N., Kaneko, K., Kitajima, A., Mitsui, T., Mu??oz, F.J., Rodr??guez-L??pez, M., Baroja-Fern??ndez, E., Pozueta-Romero, J. Plant Cell (2006) [Pubmed]
  8. Identification and molecular characterization of shrunken-2 cDNA clones of maize. Bhave, M.R., Lawrence, S., Barton, C., Hannah, L.C. Plant Cell (1990) [Pubmed]
  9. A complete ferredoxin/thioredoxin system regulates fundamental processes in amyloplasts. Balmer, Y., Vensel, W.H., Cai, N., Manieri, W., Schürmann, P., Hurkman, W.J., Buchanan, B.B. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  10. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. Qu, Q., Lee, S.J., Boos, W. J. Biol. Chem. (2004) [Pubmed]
  11. Biosynthesis of bacterial glycogen. Determination of the amino acid changes that alter the regulatory properties of a mutant Escherichia coli ADP-glucose synthetase. Kumar, A., Ghosh, P., Lee, Y.M., Hill, M.A., Preiss, J. J. Biol. Chem. (1989) [Pubmed]
  12. Covalent modification of the inhibitor binding site(s) of Escherichia coli ADP-glucose synthetase: specific incorporation of the photoaffinity analogue 8-azidoadenosine 5'-monophosphate. Larsen, C.E., Preiss, J. Biochemistry (1986) [Pubmed]
  13. Arginine294 is essential for the inhibition of Anabaena PCC 7120 ADP-glucose pyrophosphorylase by phosphate. Sheng, J., Preiss, J. Biochemistry (1997) [Pubmed]
  14. Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics. Greene, T.W., Kavakli, I.H., Kahn, M.L., Okita, T.W. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  15. Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation. Greene, T.W., Chantler, S.E., Kahn, M.L., Barry, G.F., Preiss, J., Okita, T.W. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  16. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C gene. Baecker, P.A., Furlong, C.E., Preiss, J. J. Biol. Chem. (1983) [Pubmed]
  17. Role of the conserved Lys-X-Gly-Gly sequence at the ADP-glucose-binding site in Escherichia coli glycogen synthase. Furukawa, K., Tagaya, M., Tanizawa, K., Fukui, T. J. Biol. Chem. (1993) [Pubmed]
  18. Most of ADP x glucose linked to starch biosynthesis occurs outside the chloroplast in source leaves. Baroja-Fernández, E., Muñoz, F.J., Zandueta-Criado, A., Morán-Zorzano, M.T., Viale, A.M., Alonso-Casajús, N., Pozueta-Romero, J. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  19. Relaxed sugar donor selectivity of a Sinorhizobium meliloti ortholog of the Rhizobium leguminosarum mannosyl transferase LpcC. Role of the lipopolysaccharide core in symbiosis of Rhizobiaceae with plants. Kanipes, M.I., Kalb, S.R., Cotter, R.J., Hozbor, D.F., Lagares, A., Raetz, C.R. J. Biol. Chem. (2003) [Pubmed]
  20. ADP-glucose pyrophosphorylase is located in the plastid in developing tomato fruit. Beckles, D.M., Craig, J., Smith, A.M. Plant Physiol. (2001) [Pubmed]
  21. Enzymic capacities of amyloplasts from wheat (Triticum aestivum) endosperm. Entwistle, G., Rees, T.A. Biochem. J. (1988) [Pubmed]
  22. Comparative analysis of mitochondrial and amyloplast adenylate translocators. Pozueta-Romero, J., Viale, A.M., Akazawa, T. FEBS Lett. (1991) [Pubmed]
  23. Biosynthesis of bacterial glycogen. The nature of the binding of substrates and effectors to ADP-glucose synthase. Haugen, T.H., Preiss, J. J. Biol. Chem. (1979) [Pubmed]
  24. Evidence that SNF1-related kinase and hexokinase are involved in separate sugar-signalling pathways modulating post-translational redox activation of ADP-glucose pyrophosphorylase in potato tubers. Tiessen, A., Prescha, K., Branscheid, A., Palacios, N., McKibbin, R., Halford, N.G., Geigenberger, P. Plant J. (2003) [Pubmed]
  25. Nuclear magnetic resonance studies of the solution conformation of nucleoside diphosphohexoses and their components. Lee, C.H., Sarma, R.H. Biochemistry (1976) [Pubmed]
  26. Impact of heterologous expression of Escherichia coli UDP-glucose pyrophosphorylase on trehalose and glycogen synthesis in Corynebacterium glutamicum. Padilla, L., Morbach, S., Krämer, R., Agosin, E. Appl. Environ. Microbiol. (2004) [Pubmed]
  27. Cloning of the ADPglucose pyrophosphorylase (glgC) and glycogen synthase (glgA) structural genes from Salmonella typhimurium LT2. Leung, P.S., Preiss, J. J. Bacteriol. (1987) [Pubmed]
  28. A glgC gene essential only for the first of two spatially distinct phases of glycogen synthesis in Streptomyces coelicolor A3(2). Martin, M.C., Schneider, D., Bruton, C.J., Chater, K.F., Hardisson, C. J. Bacteriol. (1997) [Pubmed]
  29. A chromosomal cluster of genes encoding ADP-glucose synthetase, glycogen synthase and phosphoglucomutase in Agrobacterium tumefaciens. Uttaro, A.D., Ugalde, R.A. Gene (1994) [Pubmed]
  30. In situ staining of activities of enzymes involved in carbohydrate metabolism in plant tissues. Sergeeva, L.I., Vreugdenhil, D. J. Exp. Bot. (2002) [Pubmed]
  31. Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. Leung, P., Lee, Y.M., Greenberg, E., Esch, K., Boylan, S., Preiss, J. J. Bacteriol. (1986) [Pubmed]
  32. Identification of Lys277 at the active site of Escherichia coli glycogen synthase. Application of affinity labeling combined with site-directed mutagenesis. Furukawa, K., Tagaya, M., Tanizawa, K., Fukui, T. J. Biol. Chem. (1994) [Pubmed]
  33. Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose-protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase. Parsons, T.F., Preiss, J. J. Biol. Chem. (1978) [Pubmed]
  34. Characterization of transgenic potato (Solanum tuberosum) tubers with increased ADPglucose pyrophosphorylase. Sweetlove, L.J., Burrell, M.M., ap Rees, T. Biochem. J. (1996) [Pubmed]
  35. PCR amplification and sequences of cDNA clones for the small and large subunits of ADP-glucose pyrophosphorylase from barley tissues. Villand, P., Aalen, R., Olsen, O.A., Lüthi, E., Lönneborg, A., Kleczkowski, L.A. Plant Mol. Biol. (1992) [Pubmed]
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