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Synthesis of Three C ‐Glycoside Analogues of UDP‐Galactopyranose as Conformational Probes for the Mutase‐Catalyzed Furanose/Pyranose Interconversion
Author(s) -
Caravano Audrey,
Vincent Stéphane P.
Publication year - 2009
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200801249
Subject(s) - chemistry , furanose , pyranose , mutase , stereochemistry , isomerization , glycosidic bond , biosynthesis , catalysis , biochemistry , enzyme , organic chemistry , ring (chemistry)
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 & Co. KGaA, 69451 Weinheim, Germany, 2009)