Section 1. XVI Symposium «Current problems of chemistry, biology and technology of natural compounds»
Why are the non-specific reactions catalyzed by Escherichia coli purine nucleoside phosphorylase not explained by classical catalysis mechanisms?
Irina D. Konstantinova 🎤
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
Ilya V. Fateev
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
Maria Ya. Berzina
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
Barbara Z. Eletskaya
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
Alexey L. Kayushin
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
Roman S. Esipov
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
Anatoly I. Miroshnikov
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Russian Federation
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Abstract
E. coli purine nucleoside phosphorylases (PNP) are often used in the enzymatic synthesis of modified nucleosides. It is known that the transglycosylation reaction is characterized by high stereo- and regio-selectivity and is environmentally friendly. The active sites of E. coli and humans PNPs have been studied for several decades. A mechanism for the catalytic process has been proposed based on X-ray structural analysis data. However, we know numerous examples of a regioselectivity lack in the synthesis of purine, fleximer, and modified benzimidazole nucleosides.
Publication Details
Published Date07/10/2026
ConferenceInternational Conference “Biologically active compounds: From chemistry to medicine”
Pages26
This article is licensed under a Creative Commons Attribution 4.0 International License.