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Chemical Compound Review

CHEMBL460741     [(2R,3S,4R,5R)-5-(2,4- dioxopyrimidin-1-yl)...

Synonyms: SureCN345577, CHEBI:28895, AR-1F5309, AC1L2R1V, AC1Q69CJ, ...
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Disease relevance of C01368


High impact information on C01368

  • Poly (U) appears to be hydrolyzed completely to 3'-UMP; both RNA and DNA appear to have some phosphodiester bonds resistant to enzyme catalyzed hydrolysis [2].
  • Isothermal titration calorimetric studies on the complexation of wild-type RNase A and the variants with 3'-UMP at pH 6.0 show that His12 and His119 contribute 1.4 and 1.1 kcal/mol to complex stability, respectively [3].
  • Theoretical probes of conformational fluctuations in S-peptide and RNase A/3'-UMP enzyme product complex [4].
  • The spin adducts generated by the reactions of OH radicals with 3'-UMP were separated by paired-ion HPLC and the separated spin adducts were identified by ESR spectroscopy [5].
  • The cyclization of 3'-AMP and 3'-UMP to the corresponding 2'-3'-cyclic phosphates proceeds in yields as high as 40-50% at 60 degrees C in pH 6 aqueous solutions in the presence of divalent metal ions [6].

Associations of C01368 with other chemical compounds

  • 1. Kinetic studies of the initial rate of hydrolysis of 2':3'-cyclic CMP show that the midpoint of the transition shifts to lower concentrations of 2':3'-cyclic CMP in the presence of the substrate analogues 3'-CMP, 5'-CMP, 3'-AMP, 3'-UMP and Pi; 2'-CMP and 2'-UMP do not cause such a shift [7].
  • 0. The RNase released mononucleotides from RNA in the order of 3'-GMP, 3'-AMP, and 3'-UMP [8].
  • The crystal structures of RNase MC1 in complex with 2'-UMP or 3'-UMP reveal that Gln9, Asn71, Leu73, and Phe80 are involved in uridine binding by hydrogen bonding and hydrophobic interactions [Suzuki et al. (2000) Biochem. Biophys. Res. Commun. 275, 572-576] [9].
  • These differences probably arise (in part) from the phosphoryl groups of 3'-UMP, dU(F)MP, and araUMP (pK(a) = 5.9) being more anionic than that of dUMP (pK(a) = 6.3) [10].

Analytical, diagnostic and therapeutic context of C01368

  • Comparison of the titration curves of the unliganded enzyme with that obtained in the presence of different concentrations of 3'-UMP shows that a second molecule of 3'-UMP can bind to the enzyme [11].
  • OH-induced free radicals in 3'-UMP and poly(U): spin-trapping and radical chromatography [5].


  1. Computer modelling studies of ribonuclease A-pyrimidine nucleotide complexes. Seshadri, K., Balaji, P.V., Rao, V.S., Vishveshwara, S. J. Biomol. Struct. Dyn. (1993) [Pubmed]
  2. Purification and properties of a light-inducible nuclease from Euglena gracilis. Small, G.D., Sturgen, R.S. Nucleic Acids Res. (1976) [Pubmed]
  3. Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding. Park, C., Schultz, L.W., Raines, R.T. Biochemistry (2001) [Pubmed]
  4. Theoretical probes of conformational fluctuations in S-peptide and RNase A/3'-UMP enzyme product complex. Straub, J.E., Thirumalai, D. Proteins (1993) [Pubmed]
  5. OH-induced free radicals in 3'-UMP and poly(U): spin-trapping and radical chromatography. Inanami, O., Kuwabara, M., Sato, F. Radiat. Res. (1987) [Pubmed]
  6. The investigation of the HCN derivative diiminosuccinonitrile as a prebiotic condensing agent. The formation of phosphate esters. Ferris, J.P., Yanagawa, H., Dudgeon, P.A., Hagan, W.J., Mallare, T.E. Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life. (1984) [Pubmed]
  7. Further evidence for an allosteric model for ribonuclease. Walker, E.J., Ralston, G.B., Darvey, I.G. Biochem. J. (1976) [Pubmed]
  8. Purification, some properties, and primary structure of a base non-specific ribonuclease from oyster (Crussdstrea grigus). Watanabe, H., Narumi, H., Inaba, T., Ohgi, K., Irie, M. J. Biochem. (1993) [Pubmed]
  9. Contribution of Gln9 and Phe80 to substrate binding in ribonuclease MC1 from bitter gourd seeds. Numata, T., Kimura, M. J. Biochem. (2001) [Pubmed]
  10. Binding of non-natural 3'-nucleotides to ribonuclease A. Jenkins, C.L., Thiyagarajan, N., Sweeney, R.Y., Guy, M.P., Kelemen, B.R., Acharya, K.R., Raines, R.T. FEBS J. (2005) [Pubmed]
  11. His ... Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymes. Quirk, D.J., Raines, R.T. Biophys. J. (1999) [Pubmed]
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