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Gene Review

deoD  -  purine nucleoside phosphorylase 1;...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4376, JW4347, pup
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Disease relevance of deoD


High impact information on deoD


Chemical compound and disease context of deoD

  • The ternary complex of purine nucleoside phosphorylase from E. coli with formycin B and a sulphate or phosphate ion crystallized in the hexagonal space group P6122 with unit cell dimensions a=123.11, c=241.22 A and three monomers per asymmetric unit [3].
  • BACKGROUND: Purine nucleoside phosphorylase (PNP) from Escherichia coli is a hexameric enzyme that catalyzes the reversible phosphorolysis of 6-amino and 6-oxopurine (2'-deoxy)ribonucleosides to the free base and (2'-deoxy)ribose-1-phosphate [6].
  • In E. coli PNP, the purine- and ribose-binding sites are generally hydrophobic, although a histidine residue from an adjacent subunit probably forms a hydrogen bond with a hydroxyl group of the sugar [6].
  • The proposed decay function was used to study effect of the interaction of E. coli purine nucleoside phosphorylase (PNP-I, the product of the deoD gene) with its specific inhibitor, viz. formycin A (FA), on fluorescence decays of ligand and enzyme tyrosine residues, in the presence of orthophosphate (P(i), a natural co-substrate) [7].

Biological context of deoD


Associations of deoD with chemical compounds


Other interactions of deoD


Analytical, diagnostic and therapeutic context of deoD

  • The difference in the specificities of these two enzymes has been utilized in gene therapy treatments in which certain prodrugs are cleaved by E. coli PNP but not the human enzyme [6].
  • Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy [5].


  1. Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1. Buxton, R.S. J. Bacteriol. (1975) [Pubmed]
  2. Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase. Bennett, E.M., Li, C., Allan, P.W., Parker, W.B., Ealick, S.E. J. Biol. Chem. (2003) [Pubmed]
  3. Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution. Koellner, G., Luić, M., Shugar, D., Saenger, W., Bzowska, A. J. Mol. Biol. (1998) [Pubmed]
  4. Transport of adenine, hypoxanthine and uracil into Escherichia coli. Burton, K. Biochem. J. (1977) [Pubmed]
  5. Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy. Modrak-Wójcik, A., Stepniak, K., Akoev, V., Zółkiewski, M., Bzowska, A. Protein Sci. (2006) [Pubmed]
  6. The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology. Mao, C., Cook, W.J., Zhou, M., Koszalka, G.W., Krenitsky, T.A., Ealick, S.E. Structure (1997) [Pubmed]
  7. A new approach to interpretation of heterogeneity of fluorescence decay: effect of induced tautomeric shift and enzyme-->ligand fluorescence resonance energy transfer. Wlodarczyk, J., Kierdaszuk, B. Biophys. Chem. (2006) [Pubmed]
  8. Overexpression of Escherichia coli genes encoding nucleoside phosphorylases in the pET/Bl21(DE3) system yields active recombinant enzymes. Esipov, R.S., Gurevich, A.I., Chuvikovsky, D.V., Chupova, L.A., Muravyova, T.I., Miroshnikov, A.I. Protein Expr. Purif. (2002) [Pubmed]
  9. Synthesis of deoxyribomononucleotides in Mollicutes: dependence on deoxyribose-1-phosphate and PPi. McElwain, M.C., Pollack, J.D. J. Bacteriol. (1987) [Pubmed]
  10. Influence of the rho-15 temperature-sensitive (ts) mutation on the expression of the deo-operon in Escherichia coli. Sukhodolets, V.V., Mironov, A.S., Linkova, E.V. Mol. Gen. Genet. (1982) [Pubmed]
  11. Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon. Schuch, R., Garibian, A., Saxild, H.H., Piggot, P.J., Nygaard, P. Microbiology (Reading, Engl.) (1999) [Pubmed]
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