Abstract
Nucleoside phosphorylases (NPases) were found to be induced in Enterobacter aerogenes DGO-04, and cytidine and cytidine 5′-monophosphate (CMP) were the best inducers. Five mmol/L to fifteen mmol/L cytidine or CMP could distinctly increase the activities of purine nucleoside phosphorylase (PNPase), uridine phosphorylase (UPase) and thymidine phosphorylase (TPase) when they were added into medium from 0 to 8 h. In the process of enzymatic synthesis of adenine arabinoside from adenine and uracil arabinoside with wet cells of Enterobacter aerogenes DGO-04 induced by cytidine or CMP, the reaction time could be shortened from 36 to 6 h. After enzymatic reaction the activity of NPase in the cells induced remained higher than that in the cells uninduced.
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References
Bzowska, A., Kulikowska, E., Shugar, D., 2000. Purine nucleoside phosphorylases: properties, functions, and clinical aspects. Pharmacology & Therapeutics, 88(3):349–425. [doi:10.1016/S0163-7258(00)00097-8]
Caradoc-Davies, T.T., Cutfield, S.M., Lamont, I.L., Cutfield, J.F., 2004. Crystal structures of Escherichia coli uridine phosphorylase in two native and three complexed forms reveal basis of substrate specificity, induced conformational changes and influence of potassium. Journal Molecular Biology, 337(2):337–354.
Esipov, R.S., Gurevich, A.I., Chuvikovsky, D.V., Chupova, L.A., Muravyova, T.I., Miroshnikov, A.I., 2002. Over-expression of Escherichia coli genes encoding nucleoside phosphorylases in the pET/B121(DE3) system yields active recombinant enzymes. Protein Expression and Purification, 24(1):56–60. [doi:10.1006/prep.2001.1524]
Giuseppina, B., Simona, C., Daniela, G., Gaetano, O., Giancarlo, T., Gabriele, Z., 2000. Recombinant Bacterial Strains for the Production of Natural Nucleosides and Modified Analogues Thereof. WO 00/39307.
Hammer-Jespersen, K., Munch-Petersen, A., Nygaard, P., Schwartz, M., 1971. Induction of enzymes involved in the catabolism of deoxyribonucleosides and ribonucleosides in Escherichia coli K12. European Journal of Biochemistry, 19(4): 533–538. [doi:10.1111/j.1432-1033.1971.tb01345.x]
Herman, M.K., 1947. Differential spectrophotometry of purine compounds by means of specific enzymes. Journal of Biological Chemistry, 167:429–443.
Jarkko, R., Tatiana, E., Seppo, L., Igor, A.M., Roman, S.E., Anatoly, I.M., 2007. An enzymatic transglycosylation of purine bases. Nucleosides Nucleotides Nucleic Acids, 26(8/9):905–909.
Kalckar, H.M., Klenow, H., 1948. Milk xanthopterin oxidase and pteroylglutamic acid. Journal of Biology Chemistry, 172:349–353.
Krenitsky, T.A., Elion, G.B., Rideout, J.E., 1979. Enzynatic Synthesis of Purine Arabinonucleosides. EP 0002192 B1.
Ling, F., Inoue, Y., Kimura, A., 1990. Purification and characterization of a novel nucleoside phosphorylase from a Klebsiella sp. and its use in the enzymatic production of adenine arabinoside. Applied and Environmental Microbiology, 56(12):3830–3834.
Ling, F., Inoue, Y., Kimura, A., 1994. Induction, purification and utilization of purine nucleoside phosphorylase and uridine phosphorylase from Klebsiella sp. Process Biochemistry, 29(5):355–361. [doi:10.1016/0032-9592(94)87004-7]
Munch-Petersen, A., 1968. On the catabolism of deoxyribonucleosides in cells and cell extracts of Eschechia coli. European Journal Biochemistry, 6(3):432–442. [doi:10.1111/j.1432-1033.1968.tb00465.x]
Robertson, B.C., Jargiello, P., Blank, J., Patricia, A.H., 1970. Genetic regulation of ribonucleoside and deoxyribonucleoside catabolism in Salmonella typhimurium. Journal of Bacteriology, 102:628–635.
Saunders, P.P., Barbara, A.W., Saunders, G.F., 1969. Purification and comparative properties of a pyrimidine nucleoside phophorylase from Bacillus stearothermophilus. Journal of Biological Chemistry, 244(13):3691–3697.
Thomsen, L.E., Pedersen, M., Nørregaard-Madsen, M., Valentin-Hansen, P., Kallipolitis, B.H., 1999. Proteinligand interaction: grafting of the uridine-specific determinants from the CytR regulator of Salmonnella typhimurium to Escherichia coli CytR. Journal Molecular Biology, 288(1):165–175. [doi:10.1006/jmbi.1999.2668]
Tozzi, M.G., Sgarrella, F., Ipata, P.L., 1981. Induction and repression of enzymes involved in exogenous purine compound utilization in Bacillus cereus. Biochimica et Biophysica Acta, 678:460–466.
Trelles, J.A., Fernández-Lucas, J., Condezo, L.A., Sinisterra, J.V., 2004. Nucleoside synthesis by immobilised bacterial whole cells. Journal of Molecular Catalysis B: Enzymatic, 30(5–6):219–227. [doi:10.1016/j.molcatb.2004.06.001]
Utagawa, T., Hirokazu, M., Fumihiro, Y., Akihiro, Y., Koji, M., 1985. Microbiological synthesis of adenine arabinoside. Agricultural and Biological Chemistry, 49(4):1053–1058.
Vita, A., Amici, A., Magni, G., 1983. Induction of pyrimidine nucleosides metabolizing enzymes in E. coli B. Italy Journal Biochemistry, 32(3):145–151.
Zolotukhina, M., Ovcharova, I., Eremina, S., Errais, L., Mironov, A.S., 2003. Comparison of the structure and regulation of the udp gene of Vibrio cholerae, Yersinia pseudotuberculosis, Salmonella typhimurium, and Escherichia coli. Research in Microbiology, 154(7):510–520. [doi:10.1016/S0923-2508(03)00125-6]
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Project (No. 07C26213101283) supported by the Innovation Fund for Technology Based Firms from the Ministry of Science and Technology of China
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Wei, Xk., Ding, Qb., Zhang, L. et al. Induction of nucleoside phosphorylase in Enterobacter aerogenes and enzymatic synthesis of adenine arabinoside. J. Zhejiang Univ. Sci. B 9, 520–526 (2008). https://doi.org/10.1631/jzus.B0710618
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DOI: https://doi.org/10.1631/jzus.B0710618
Key words
- Nucleoside phosphorylase (NPase)
- Enterobacter aerogenes
- Cytidine
- Cytidine 5′-monophosphate (CMP)
- Adenine arabinoside