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Gene Review

cdd  -  cytidine/deoxycytidine deaminase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2136, JW2131
 
 
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Disease relevance of cdd

 

High impact information on cdd

 

Chemical compound and disease context of cdd

 

Biological context of cdd

 

Anatomical context of cdd

  • Expression of CDD in 20 human cancer cell lines was highly variable and not related to its expression in normal tissues [5].
  • Our results demonstrate that CDD can be up-regulated by vitamin D3 in some solid tumor cell lines [5].
  • Northern blot analysis demonstrated high levels of CDD mRNA in leukocytes and moderate levels in liver, kidney, placenta, spleen and lung [5].
 

Associations of cdd with chemical compounds

 

Other interactions of cdd

  • By the use of phage lambda (lac, Mu) the promoter for the cdd gene has been fused to lacZ [2].
 

Analytical, diagnostic and therapeutic context of cdd

  • By using site-directed mutagenesis of the cdd-lacZ' fusion, it was shown that frameshifting occurred at the sequence CGA AAG, 9 bp upstream of the in-frame cdd stop codon, and that it was stimulated by a Shine-Dalgarno-like sequence located 14 bp upstream of the shift site [3].
  • In the present work, we determined the thermodynamic changes associated with the equilibrium binding of inhibitors by cytidine deaminase by isothermal titration calorimetry and van't Hoff analysis of the temperature dependence of their inhibition constants [21].
  • We show by sequence alignment, molecular modelling and mutagenesis, that it is related in crystal structure to the cytidine deaminase of Escherichia coli (ECCDA) [22].
  • The recombinant CDA has been purified to homogeneity by a rapid procedure consisting of heat inactivation followed by affinity chromatography [23].
  • The protein expressed in E. coli showed high cytidine deaminase activity and its molecular mass was estimated to be 57 kDa by gel filtration and 16 kDa by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) [23].

References

  1. CRP/cAMP- and CytR-regulated promoters in Escherichia coli K12: the cdd promoter. Valentin-Hansen, P., Holst, B., Josephsen, J., Hammer, K., Albrechtsen, B. Mol. Microbiol. (1989) [Pubmed]
  2. Fusion of the lac genes to the promotor for the cytidine deaminase gene of Escherichia coli K-12. Josephsen, J., Hammer-Jespersen, K. Mol. Gen. Genet. (1981) [Pubmed]
  3. Ribosomal -1 frameshifting during decoding of Bacillus subtilis cdd occurs at the sequence CGA AAG. Mejlhede, N., Atkins, J.F., Neuhard, J. J. Bacteriol. (1999) [Pubmed]
  4. The action of bacterial cytidine deaminase on 5,6-dihydrocytidine. Evans, B.E., Mitchell, G.N., Wolfenden, R. Biochemistry (1975) [Pubmed]
  5. Expression of cytidine deaminase in human solid tumors and its regulation by 1 alpha,25-dihydroxyvitamin D3. Watanabe, S., Uchida, T. Biochim. Biophys. Acta (1996) [Pubmed]
  6. Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site. Navaratnam, N., Bhattacharya, S., Fujino, T., Patel, D., Jarmuz, A.L., Scott, J. Cell (1995) [Pubmed]
  7. A whole genome approach to in vivo DNA-protein interactions in E. coli. Wang, M.X., Church, G.M. Nature (1992) [Pubmed]
  8. Activation-induced cytidine deaminase (AID) can target both DNA strands when the DNA is supercoiled. Shen, H.M., Storb, U. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  9. Cloning and verification of the Lactococcus lactis pyrG gene and characterization of the gene product, CTP synthase. Wadskov-Hansen, S.L., Willemoës, M., Martinussen, J., Hammer, K., Neuhard, J., Larsen, S. J. Biol. Chem. (2001) [Pubmed]
  10. Origin of tight binding of a near-perfect transition-state analogue by cytidine deaminase: implications for enzyme catalysis. Guo, H., Rao, N., Xu, Q., Guo, H. J. Am. Chem. Soc. (2005) [Pubmed]
  11. The sfiX, rfe and metN genes of Salmonella typhimurium and their involvement in the His(c) pleiotropic response. Mouslim, C., Cano, D.A., Casadesús, J. Mol. Gen. Genet. (1998) [Pubmed]
  12. Binding of pyrimidin-2-one ribonucleoside by cytidine deaminase as the transition-state analogue 3,4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity. Frick, L., Yang, C., Marquez, V.E., Wolfenden, R. Biochemistry (1989) [Pubmed]
  13. Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase. Song, B.H., Neuhard, J. Mol. Gen. Genet. (1989) [Pubmed]
  14. Major contribution of a carboxymethyl group to transition-state stabilization by cytidine deaminase: mutation and rescue. Carlow, D.C., Smith, A.A., Yang, C.C., Short, S.A., Wolfenden, R. Biochemistry (1995) [Pubmed]
  15. The role of zinc in Bacillus subtilis cytidine deaminase. Mejlhede, N., Neuhard, J. Biochemistry (2000) [Pubmed]
  16. Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene. Yang, C., Carlow, D., Wolfenden, R., Short, S.A. Biochemistry (1992) [Pubmed]
  17. Mapping of markers in the gyrA-his region of Escherichia coli. Middendorf, A., Schweizer, H., Vreemann, J., Boos, W. Mol. Gen. Genet. (1984) [Pubmed]
  18. Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex. Betts, L., Xiang, S., Short, S.A., Wolfenden, R., Carter, C.W. J. Mol. Biol. (1994) [Pubmed]
  19. Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis. Xiang, S., Short, S.A., Wolfenden, R., Carter, C.W. Biochemistry (1996) [Pubmed]
  20. Mutagenicity of the cytidine analog zebularine in Escherichia coli. Lee, G., Wolff, E., Miller, J.H. DNA Repair (Amst.) (2004) [Pubmed]
  21. Site-bound water and the shortcomings of a less than perfect transition state analogue. Snider, M.J., Wolfenden, R. Biochemistry (2001) [Pubmed]
  22. Molecular modelling and the biosynthesis of apolipoprotein B containing lipoproteins. Scott, J., Navaratnam, N., Carter, C. Atherosclerosis (1998) [Pubmed]
  23. Recombinant human cytidine deaminase: expression, purification, and characterization. Vincenzetti, S., Cambi, A., Neuhard, J., Garattini, E., Vita, A. Protein Expr. Purif. (1996) [Pubmed]
 
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