Crystallization and preliminary X-ray study of Vibrio cholerae uridine phosphorylase in complex with 6-methyluracil
作者： Igor I Prokofev , Alexander A Lashkov , Azat G Gabdulkhakov , Mariya V Dontsova , Tatyana A Seregina
DOI: 10.1107/S2053230X13031877
关键词:
摘要: Uridine phosphorylase catalyzes the phosphorolysis of ribonucleosides, with nitrogenous base and ribose 1-phosphate as products. Additionally, it reverse reaction synthesis ribonucleosides from a base. However, enzyme does not catalyze nucleosides when substrate is substituted at 6-position, such 6-methyluracil (6-MU). In order to explain this fact, essential investigate three-dimensional structure complex 6-MU uridine phosphorylase. pharmaceutical agent that improves tissue nutrition enhances cell regeneration by normalization nucleotide exchange in humans. used for treatment diseases gastrointestinal tract, including infectious diseases. Here, procedures obtain pathogenic bacterium Vibrio cholerae (VchUPh), purification enzyme, crystallization VchUPh 6-MU, X-ray data collection preliminary analysis VchUPh–6-MU atomic resolution are reported.
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desy.de参考文章(23)
M H el Kouni, F N Naguib, J G Niedzwicki, M H Iltzsch, S Cha, Uridine phosphorylase from Schistosoma mansoni. Journal of Biological Chemistry. ,vol. 263, pp. 6081- 6086 ,(1988) , 10.1016/S0021-9258(18)68752-6
Konstantin A Petrov, Lilia O Yagodina, Guzel R Valeeva, Natalya I Lannik, Alexandra D Nikitashina, Albert A Rizvanov, Vladimir V Zobov, Ellya A Bukharaeva, Vladimir S Reznik, Eugeny E Nikolsky, František Vyskočil, None, Different sensitivities of rat skeletal muscles and brain to novel anti-cholinesterase agents, alkylammonium derivatives of 6-methyluracil (ADEMS) British Journal of Pharmacology. ,vol. 163, pp. 732- 744 ,(2011) , 10.1111/J.1476-5381.2011.01211.X
Peter W. Woodman, Awni M. Sarrif, Charles Heidelberger, Specificity of pyrimidine nucleoside phosphorylases and the phosphorolysis of 5-fluoro-2'-deoxyuridine. Cancer Research. ,vol. 40, pp. 507- 511 ,(1980)
Alexander A. Lashkov, Nadezhda E. Zhukhlistova, Azat H. Gabdoulkhakov, Alexander A. Shtil, Roman G. Efremov, Christian Betzel, Al'bert M. Mikhailov, The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. Acta Crystallographica Section D-biological Crystallography. ,vol. 66, pp. 51- 60 ,(2010) , 10.1107/S0907444909044175
Johan Christian LEER, Karin HAMMER-JESPERSEN, Marianne SCHWARTZ, Uridine Phosphorylase from Escherichia coli FEBS Journal. ,vol. 75, pp. 217- 224 ,(1977) , 10.1111/J.1432-1033.1977.TB11520.X
Joseph El-On, Louis Weinrauch, Combination therapy (monomycine and methyluracil) in Leishmania cutis. International Journal of Dermatology. ,vol. 29, pp. 232- 232 ,(1990) , 10.1111/J.1365-4362.1990.TB03812.X
E.Yu. Morgunova, A.M. Mikhailov, A.N. Popov, E.V. Blagova, E.A. Smirnova, B.K. Vainshtein, Ch. Mao, Sh.R. Armstrong, S.E. Ealick, A.A. Komissarov, E.V. Linkova, A.A. Burlakova, A.S. Mironov, V.G. Debabov, Atomic structure at 2.5 Å resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice FEBS Letters. ,vol. 367, pp. 183- 187 ,(1995) , 10.1016/0014-5793(95)00489-V
Olaf H. Temmink, Michiel de Bruin, Annelies W. Turksma, Silvia Cricca, Adrie C. Laan, Godefridus J. Peters, Activity and substrate specificity of pyrimidine phosphorylases and their role in fluoropyrimidine sensitivity in colon cancer cell lines. The International Journal of Biochemistry & Cell Biology. ,vol. 39, pp. 565- 575 ,(2007) , 10.1016/J.BIOCEL.2006.10.009
Maria Zolotukhina, Irina Ovcharova, Svetlana Eremina, Liubov Errais Lopes, Alexander S Mironov, None, Comparison of the structure and regulation of the udp gene of Vibrio cholerae, Yersinia pseudotuberculosis, Salmonella typhimurium, and Escherichia coli. Research in Microbiology. ,vol. 154, pp. 510- 520 ,(2003) , 10.1016/S0923-2508(03)00125-6
Estera Krajewska, David Shugar, Pyrimidine ribonucleoside phosphorylase activity vs 5- and/or 6-substituted uracil and uridine analogues, including conformational aspects Biochemical Pharmacology. ,vol. 31, pp. 1097- 1102 ,(1982) , 10.1016/0006-2952(82)90348-3