Synthesis of Three <i>C</i>‐Glycoside Analogues of UDP‐Galactopyranose as Conformational Probes for the Mutase‐Catalyzed Furanose/Pyranose Interconversion

Abstract

Abstract UDP‐galactopyranose mutase (UGM) catalyzes the isomerization of UDP‐galacto pyranose (UDP‐Gal p ) into UDP‐galacto furanose (UDP‐Gal f ), an essential step of the mycobacterial cell wall biosynthesis. In order to probe the UGM binding pocket, we synthesized the α‐ and β‐ C ‐glycosidic analogues of UDP‐galacopyranose along with the corresponding UDP‐ exo ‐galactal. Preliminary inhibition evaluation indicated that UDP‐ exo ‐galactal inhibits UGM with a binding affinity similar to that of UDP‐α‐ C ‐galactopyranose.(© Wiley‐VCH Verlag GmbH &amp; Co. KGaA, 69451 Weinheim, Germany, 2009)