Substrate Specificity of a Purine Nucleoside Phosphorylase from Aeromonas hydrophila Toward 6-Substituted Purines and its Use as a Biocatalyst in the Synthesis of the Corresponding Ribonucleosides

Title:Substrate Specificity of a Purine Nucleoside Phosphorylase from Aeromonas hydrophila Toward 6-Substituted Purines and its Use as a Biocatalyst in the Synthesis of the Corresponding Ribonucleosides

Volume: 19 Issue: 22

Author(s): Daniela Ubiali, Carlo F. Morelli, Marco Rabuffetti, Giulia Cattaneo, Immacolata Serra, Teodora Bavaro, Alessandra M. Albertini and Giovanna Speranza

Affiliation:

Keywords: Purine nucleoside phosphorylase, transglycosylation, chemoenzymatic synthesis, 6-substituted purine ribonucleosides, Aeromonas hydrophila.

Abstract: A purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) was found to catalyze the regio- and stereoselective transfer of the ribofuranosyl moiety from 7-methylguanosine iodide (1) to a library of 6- substituted purines, resulting in moderate to high conversions (18-65%) into their ribonucleoside counterparts (26- 34, 36-49). Exploring of substrate recognition by AhPNP with regard to 6-position of purine base provided the necessary information to exploit this biocatalyst for the chemoenzymatic synthesis of nucleoside analogues through a transglycosylation reaction.

Cite this article as:

Ubiali Daniela, Morelli F. Carlo, Rabuffetti Marco, Cattaneo Giulia, Serra Immacolata, Bavaro Teodora, Albertini M. Alessandra and Speranza Giovanna, Substrate Specificity of a Purine Nucleoside Phosphorylase from Aeromonas hydrophila Toward 6-Substituted Purines and its Use as a Biocatalyst in the Synthesis of the Corresponding Ribonucleosides, Current Organic Chemistry 2015; 19 (22) . https://dx.doi.org/10.2174/1385272819666150807191212