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.
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 / D. Ubiali, C. Morelli, M. Rabuffetti, G. Cattaneo, I. Serra, T. Bavaro, A. Albertini, G. Speranza. - In: CURRENT ORGANIC CHEMISTRY. - ISSN 1385-2728. - 19:22(2015), pp. 2220-2225.
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
C. MorelliSecondo
;M. Rabuffetti;I. Serra;G. Speranza
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.Pubblicazioni consigliate
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