Substrate specificity of uridine and purine nucleoside phosphorylases of the Escherichia coli whole cells

Authors

  • A. I. Zintchenko Institute of Microbiology, Academy of Sciences of the Byelorussian SSR Minsk, USSR Author
  • L. A. Eroshevskaya Institute of Microbiology, Academy of Sciences of the Byelorussian SSR Minsk, USSR Author
  • V. N. Barai Institute of Microbiology, Academy of Sciences of the Byelorussian SSR Minsk, USSR Author
  • I. A. Mikhailopulo Institute of Bioorganic Chemistry, Academy of Sciences of the Byelorussian SSR Minsk, USSR Author

DOI:

https://doi.org/10.7124/bc.00023C

Abstract

Substrate specificity of uridine and purine nucleoside phosphorylases of the whole cells of Escherichia coli BM-11 has been studied monitoring phosphorolysis of uridine and a series of its analogues modified in the carbohydrate moiety to uracil and pentofuranose-I-phosphate, and synthesis of corresponding adenine nucleosides. Both enzymes reveal similar requirements to the structure and stereochemistry of uracil nucleosides and of the pentofuranose-1-phosphates, respectively, namely: a) modifications at C-3' decrease the substrate activity to a greater extent as compared with the same modifications at C-2'; the order of substrate activity in the case of modifications at C-2' and C-3' is OH> H> NH2> OH-ara (xylo)» 2'(3')-C-methyl; b) substitution of a methyl group for one of the protons at carbon atom of 5'-CH?OH group does not lead to an essential alterations of the substrate activity in such analogues in comparison with the natural substrates — uridine and ribofuranose-1-phosphate, respectively.

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Published

1988-11-20

Issue

Section

Cell Biology