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

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

Journal Name: Current Organic Chemistry

Volume 19 , Issue 22 , 2015

Submit Manuscript
Submit Proposal

Graphical Abstract:


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.

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

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 19
ISSUE: 22
Year: 2015
Page: [2220 - 2225]
Pages: 6
DOI: 10.2174/1385272819666150807191212
Price: $58

Article Metrics

PDF: 29