Substrate specificity of purine nucleoside phosphorylase E. coli in phosphorolysis reactions of purine ribonucleotides containing a cyclic terpene fragment

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Abstract

Bacterial purine nucleoside phosphorylase (PNP) E. coli can be considered as an attractive model enzyme for investigation of metabolism and stability of biologically active nucleosides in a cell. This work is devoted to the investigation of the substrate specificity of E. coli PNP in the reactions of phosphorolytic cleavage of the glycoside bond in adenosine derivatives containing a cyclic terpene fragment as precursors for the production of biologically active purine derivatives. A number of N6-terpene substituted adenosine derivatives with different structures of the hydrocarbon substituent were obtained. By measuring the kinetic parameters of the phosphorolysis reaction, it was shown that adenosine derivatives containing a bicyclic hydrocarbon fragment bind to the enzyme more efficiently than a monocyclic derivative. The obtained results make it possible to produce new purine derivatives containing a lipophilic terpene fragment under mild reaction conditions.

About the authors

A. A. Kozlova

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Moscow, 119991 Russia

V. E. Oslovsky

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Moscow, 119991 Russia

M. A. Varga

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Moscow, 119991 Russia

C. S. Alexeev

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Moscow, 119991 Russia

M. S. Drenichev

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: mdrenichev@mail.ru, room517@eimb.ru
Moscow, 119991 Russia

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