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C ‐Glycosidic UDP‐GlcNAc Analogues as Inhibitors of UDP‐GlcNAc 2‐Epimerase
Author(s) -
Stolz Florian,
Blume Astrid,
Hinderlich Stephan,
Reutter Werner,
Schmidt Richard R.
Publication year - 2004
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.200400197
Subject(s) - chemistry , glycosidic bond , stereochemistry , neuraminic acid , moiety , enzyme , substrate (aquarium) , biosynthesis , biochemistry , glycoprotein , oceanography , geology
The first step in the biosynthesis of neuraminic acid, the “epimerisation” of UDP‐GlcNAc to ManNAc, is catalyzed by UDP‐GlcNAc 2‐epimerase. In this paper we report the synthesis of the C ‐glycosidic UDP‐GlcNAc analogues 1 − 5 as substrate‐based inhibitors of this enzyme. The focus is on the optimal distance and geometry of the connection between the sugar and the UDP‐moiety, which are both important for recognition by UDP‐GlcNAc 2‐epimerase. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004)