ABSTRACT
Abstract ................................................................................................. 263 10.1 Introduction ................................................................................ 264 10.2 Materials and Methods ............................................................... 265 10.3 Results and Discussion .............................................................. 268 10.4 Conclusion ................................................................................. 271 Keywords .............................................................................................. 272 References ............................................................................................. 272
ABSTRACT
The method raising efficiency of synthesis in recombinant Escherichia coli cells of pyrimidine nucleoside phosphorylase (PyrNPase) from
Thermusthermophilus by inserting silent mutations into initial fragment of gene encoding this enzyme has been described. It was proposed to increase temperature inducing PyrNPase synthesis by bacterial cells up to 42°C. Ability of mutant PyrNPase (mutPyrNPase) to catalyze phosphorolysis of 3′-fluoro-3′-deoxyuridine and 3′-fluoro-2,’3′-dideoxythymidine was demonstrated. Recombinant nucleoside phosphorylases were originally engaged for synthesis of purine fluoronucleosides such as 3′-fluoro-3′-deoxyadenosine, 3′-fluoro-3′-deoxy-2-aminoadenosine, 3′-fluoro-3′-deoxyguanosine, 3′-fluoro2,’3′-dideoxy-2-fluoroadenosine, 3′-fluoro-2,’3′-dideoxy-2-chloroadenosine, 3′-fluoro-3′-deoxy-2-fluoroadenosine, 3′-fluoro-3′-deoxy-2-chloroadenosine.
