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.
Ubiali, D., Morelli, C., Rabuffetti, M., Cattaneo, G., Serra, I., Bavaro, T., et al. (2015). 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, 19(22), 2220-2225 [10.2174/1385272819666150807191212].
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
Serra I.;
2015
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.
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