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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

3'-CMP     [(2R,3S,4R,5R)-5-(4-amino-2- oxo-pyrimidin...

Synonyms: SureCN79966, CHEMBL258728, AG-K-93131, CHEBI:53013, CTK8C5691, ...
 
 
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High impact information on 3'-CMP

  • We have investigated these kinetics by determining 3'-CMP formation both spectrophotometrically and by a highly specific and quantitative chemical sampling method [1].
  • The circular-dichroism and proton-magnetic-resonance spectra of complexes of ribonuclease A with dihydrouridine 3'-phosphate, 2'- and 3'-CMP, arabinosyl-3'-CMP, 1-(2-hydroxyethyl)cytosine 2'-phosphate and 1-(3-hydroxypropyl)cytosine 3'-phosphate were studied [2].
  • The apparent free energy (deltaGapp) and enthalpy changes (deltaHB) associated with the interaction of 3'-cytosine monophosphate (3'-CMP) and ribonuclease A (RNase) are reported for the pH range 4--9, T = 25 degrees, mu = 0.05 [3].
  • The refolding rates are different for the two protein domains and vary as a function of pH and presence of the inhibitor 3'-CMP [4].
  • CONCLUSIONS: The combination of progress curve analysis and ITC allowed rapid and facile measurement of the kinetic parameters for catalytic conversion of cCMP to 3'-CMP by RNase-A, a reaction complicated by end-product inhibition [5].
 

Biological context of 3'-CMP

  • The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules [6].
  • We show that the differentiation of the progress curve for the ribonuclease-catalyzed hydrolysis of 2',3'-cyclic cytidine monophosphate reveals strong product inhibition by 3'-CMP, and this product inhibition accounts for the large discrepancies reported in the literature for the value of Km for this substrate [7].
 

Associations of 3'-CMP with other chemical compounds

  • The stoichiometry and association constant for 3'-CMP and 5'-AMP at pH 7.0 were also determined [8].
  • This indicates that the interaction at the O(2')H [or O(2')] sites of ribonucleotides causes the two forms of complexes of 3'-UMP and 3'-CMP with RNase A [9].
 

Gene context of 3'-CMP

 

Analytical, diagnostic and therapeutic context of 3'-CMP

  • 1,10-Phenanthroline-platinum(II)-ethylenediamine ( PEPt ) forms a crystalline complex with cytidine-3'-phosphate (3'-CMP) and its structure has been determined by X-ray crystallography [11].
  • The results of this analysis are consistent with the calorimetric and potentiometric titration results for the free enzyme and its 3'-CMP complex reported in the previous paper (M [3].
  • The parameters describing the binding of the inhibitor 3'-CMP (Ka and delta H) as monitored by spectrophotometry and calorimetry were not significantly affected after immobilization [4].

References

  1. The subsites structure of bovine pancreatic ribonuclease A accounts for the abnormal kinetic behavior with cytidine 2',3'-cyclic phosphate. Moussaoui, M., Nogués, M.V., Guasch, A., Barman, T., Travers, F., Cuchillo, C.M. J. Biol. Chem. (1998) [Pubmed]
  2. The nature of the circular-dichoric spectra of complexes between ribonuclease A and nucleotides. Dudkin, S.M., Karabashyan, L.V., Karpeisky, M.Y., Mikhailov, S.N., Padyukova, N.S., Sakharovsky, V.G. Biochem. J. (1977) [Pubmed]
  3. The pH dependence of the thermodynamics of the interaction of 3'-cytidine monophosphate with ribonuclease A. Flogel, M., Biltonen, R.L. Biochemistry (1975) [Pubmed]
  4. Decoupling of melting domains in immobilized ribonuclease A. Rialdi, G., Battistel, E. Proteins (1994) [Pubmed]
  5. Isothermal titration calorimetric study of RNase-A kinetics (cCMP --> 3'-CMP) involving end-product inhibition. Spencer, S.D., Raffa, R.B. Pharm. Res. (2004) [Pubmed]
  6. The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules. Zegers, I., Maes, D., Dao-Thi, M.H., Poortmans, F., Palmer, R., Wyns, L. Protein Sci. (1994) [Pubmed]
  7. The analysis of enzyme progress curves by numerical differentiation, including competitive product inhibition and enzyme reactivation. Koerber, S.C., Fink, A.L. Anal. Biochem. (1987) [Pubmed]
  8. Affinity chromatography study of the interaction of ribonucleotides with bovine pancreatic ribonuclease covalently bound to Sepharose 4B. Nogués, M.V., Guasch, A., Alonso, J., Cuchillo, C.M. J. Chromatogr. (1983) [Pubmed]
  9. Interaction of substrate analogs with bovine pancreatic ribonuclease A as studied by 1H nuclear magnetic resonance. Tanokura, M. J. Biochem. (1983) [Pubmed]
  10. A calorimetric approach to the study of the interactions of cytidine-3'-phosphate with bovine seminal ribonuclease. Ambrosino, R., Barone, G., Castronuovo, G., Cultrera, O., Di Donato, A., Elia, V. Biopolymers (1989) [Pubmed]
  11. A crystalline end product produced by the hydrolytic cleavage of an RNA-like fragment by an organometallointercalator: 1,10-phenanthroline-platinum(II)-ethylenediamine-cytidine 3' monophosphate. Vijay-Kumar, S., Sakore, T.D., Sobell, H.M. Nucleic Acids Res. (1984) [Pubmed]
 
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