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Chemical Compound Review

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

Synonyms: CHEMBL576739, SureCN146700, AG-J-05318, A9272_SIGMA, CHEBI:28931, ...
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Disease relevance of Adenosine 3'-phosphate

  • The enzyme from Bordetella pertussis was relatively insensitive to inhibition by "P"-site agonists, exhibiting a rank order of potency of 2'd3'AMP greater than 3'-AMP greater than 2',5'-ddAdo approximately Ado approximately 2'-dAdo, with IC50 values for 2'd3'AMP and 3'-AMP of 1-3 mM [1].
  • Polynucleotide kinase (bacteriophage-T4-infected Escherichia coli B) catalyses the transfer of the [gamma-16O,17O,18O]phosphoryl group from 5'[gamma(S)-16O,17O,18O]ATP to 3'-AMP with inversion of configuration at the phosphorus atom [2].

High impact information on Adenosine 3'-phosphate

  • Further biochemical characterization of SurE revealed that it has a broad substrate specificity and can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP [3].
  • The site of hydrolysis by rabbit reticulocyte peptidyl-tRNA hydrolase is the 3'-AMP terminus of susceptible tRNA substrates [4].
  • Reticulocyte peptidyl-tRNA hydrolase also hydrolyzes th 3'-AMP terminus of deacylated tRNA [4].
  • The tRNA product of peptidyl-tRNA hydrolase action is tRNA missing only its 3'-AMP terminus (tRNA(c-c)), since reaminoacylation requires tRNA nucleotidyltransferase but not CTP [4].
  • 3'-AMP levels also varied significantly among rat tissues, with spleen having the highest levels (approximately 280 nmol/g), kidney, liver, heart, and brain having decreasing 3'-AMP content, and skeletal muscle levels being immeasureably low (less than 0.1 nmol/g) [5].

Biological context of Adenosine 3'-phosphate

  • Sets of limiting chemical shifts and coupling values were also obtained for ApA and constituent monomers 3'-AMP and 5'-AMP at infinite dilution and at identical ionization states for assessment of dimerization effects [6].
  • Additionally, lysine modification was accompanied by a concomitant loss of all the activities of the enzyme, indicating the presence of a common catalytic site responsible for the hydrolysis of single-stranded DNA, RNA and 3'-AMP [7].
  • Expression of luteinising hormone-beta subunit chloramphenicol acetyltransferase (LH-beta-CAT) fusion gene in rat pituitary cells: induction by cyclic 3'-adenosine monophosphate (cAMP) [8].
  • The clay mineral catalysis of the cyclization of adenosine-3'-phosphate was investigated using homoionic montmorillonites [9].
  • Thermal inactivation studies indicate that the active site conformations for pNPP and 3'-AMP hydrolytic activities are different [10].

Anatomical context of Adenosine 3'-phosphate

  • That is, ameloblasts incubated at pH 5.0 with 3'-AMP showed heavy deposits of reaction product at many sites throughout the cell, including most lysosomal dense bodies, the Golgi saccules, the GERL system, most secretory granules, the nucleus, and extensively throughout the endoplasmic reticulum [11].
  • From these results, 3'-AMP forming enzyme(s) in rat liver mitochondria could be classified as acid exoribonuclease, which mainly existed in an active form [12].
  • The results obtained suggested that iron loading might induce significant decrease in hepatic and splenic ATP levels via malfunction of their mitochondria and might lead dissociation of RNase-RNase inhibitor complex to activate 3'-AMP forming enzyme in both tissues [13].

Associations of Adenosine 3'-phosphate with other chemical compounds

  • DISN effects the cyclization of 3'-adenosine monophosphate to adenosine 2', 3'-cyclic phosphate in up to 39% yield [9].
  • Crystal structures of adenine-specific Ustilago sphaerogena ribonuclease U2 complexed with the substrate analogues, d(ApG), d(ApGpG), and d(ApGpC), with the intermediate analogue, 2',3'-O-isopropylidene-adenosine, and with the product, 3'-AMP, have been determined [14].
  • A non-specific acid phosphatase (APase) hydrolysing L-tyrosine-O-phosphate and 3'-AMP was purified to electrophoretic homogeneity from mature lentil seeds with apparent native molecular mass of 100 kDa and subunit molecular mass of 24 kDa [10].
  • 0. The RNase released mononucleotides from RNA in the order of 3'-UMP, 3'-GMP and 3'-AMP [15].

Gene context of Adenosine 3'-phosphate


Analytical, diagnostic and therapeutic context of Adenosine 3'-phosphate


  1. Inhibition of Bordetella pertussis and Bacillus anthracis adenylyl cyclases by polyadenylate and "P"-site agonists. Johnson, R.A., Shoshani, I. J. Biol. Chem. (1990) [Pubmed]
  2. The stereochemical course of phosphoryl transfer catalysed by polynucleotide kinase (bacteriophage-T4-infected Escherichia coli B). Jarvest, R.L., Lowe, G. Biochem. J. (1981) [Pubmed]
  3. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N.N., Kitagawa, M., Mori, H., Savchenko, A., Yakunin, A.F. J. Biol. Chem. (2004) [Pubmed]
  4. The site of hydrolysis by rabbit reticulocyte peptidyl-tRNA hydrolase is the 3'-AMP terminus of susceptible tRNA substrates. Gross, M., Crow, P., White, J. J. Biol. Chem. (1992) [Pubmed]
  5. Tissue levels, source, and regulation of 3'-AMP: an intracellular inhibitor of adenylyl cyclases. Bushfield, M., Shoshani, I., Johnson, R.A. Mol. Pharmacol. (1990) [Pubmed]
  6. Conformational properties of adenylyl-3' leads to 5'-adenosine in aqueous solution. Kondo, N.S., Danyluk, S.S. Biochemistry (1976) [Pubmed]
  7. Active-site characterization of S1 nuclease. I. Affinity purification and influence of amino-group modification. Gite, S., Reddy, G., Shankar, V. Biochem. J. (1992) [Pubmed]
  8. Expression of luteinising hormone-beta subunit chloramphenicol acetyltransferase (LH-beta-CAT) fusion gene in rat pituitary cells: induction by cyclic 3'-adenosine monophosphate (cAMP). Clayton, R.N., Lalloz, M.R., Salton, S.R., Roberts, J.L. Mol. Cell. Endocrinol. (1991) [Pubmed]
  9. The prebiotic chemistry of nucleotides. Ferris, J.P., Yanagawa, H., Hagan, W.J. Orig. Life (1984) [Pubmed]
  10. A histidine thiol 100 kDa, tetrameric acid phosphatase from lentil, Lens esculenta, seeds with the characteristics of protein tyrosine phosphatases. Roknabadi, S.M., Bose, S.K., Taneja, V. Biochim. Biophys. Acta (1999) [Pubmed]
  11. Ultrastructural localization of coenzyme A phosphatase (CoA-Pase) activity to the GERL system in secretory ameloblasts of the rat incisor. Smith, C.E. J. Histochem. Cytochem. (1981) [Pubmed]
  12. A specific and rapid method for determination of adenosine 3'-monophosphate (3'-AMP) content and 3'-AMP forming enzyme activity in rat liver mitochondria, using reversed-phase HPLC with fluorescence detection. Fujimori, H., Sato, R., Yasuda, M., Pan-Hou, H. Biol. Pharm. Bull. (1998) [Pubmed]
  13. Effect of iron lactate overloading on adenine nucleotide levels and adenosine 3'-monophosphate forming enzyme in rat liver and spleen. Fujimori, H., Ozaki, K., Matsuura, T., Matsushima, S., Narama, I., Pan-Hou, H. Biol. Pharm. Bull. (2004) [Pubmed]
  14. Crystal structures of nucleic acid complexes of ribonuclease U2. Noda, N., Noguchi, S., Satow, Y. Nucleic Acids Symp. Ser. (1997) [Pubmed]
  15. Purification, and properties of a base non-specific acid ribonuclease from bullfrog (Rana catesbeiana). Yagi, H., Kobayashi, H., Inokuchi, N., Koyama, T., Irie, M. Biol. Pharm. Bull. (1995) [Pubmed]
  16. Mitochondrial nicotinamide nucleotide transhydrogenase: active site modification by 5'-[p-(fluorosulfonyl)benzoyl]adenosine. Phelps, D.C., Hatefi, Y. Biochemistry (1985) [Pubmed]
  17. Gas-phase hydrogen/deuterium exchange of positively charged mononucleotides by use of Fourier-transform ion cyclotron resonance mass spectrometry. Green-Church, K.B., Limbach, P.A., Freitas, M.A., Marshall, A.G. J. Am. Soc. Mass Spectrom. (2001) [Pubmed]
  18. A unique surface membrane anchored purine-salvage enzyme is conserved among a group of primitive eukaryotic human pathogens. Debrabant, A., Bastien, P., Dwyer, D.M. Mol. Cell. Biochem. (2001) [Pubmed]
  19. A specific polyadenylase from Escherichia coli K12. Antoniades, D., Antonoglou, O. Biochim. Biophys. Acta (1977) [Pubmed]
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