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Towards New MraY Inhibitors: A Serine Template for Uracil and 5‐Amino‐5‐deoxyribosyl Scaffolding
Author(s) -
Le Corre Laurent,
GravierPelletier Christine,
Le Merrer Yves
Publication year - 2007
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.200700527
Subject(s) - chemistry , translocase , uracil , reductive amination , serine , alkylation , combinatorial chemistry , deoxyribose , stereochemistry , moiety , biochemistry , enzyme , nucleic acid , catalysis , dna , chromosomal translocation , gene
The bacterial translocase MraY is a good target for the development of new antitbiotics as it is ubiquitous and essential for bacterial growth. The goal of this work was the synthesis of simplified analogues of naturally occurring inhibitors of this enzyme to investigate the essential character of the uridine moiety of these inhibitors with regards to biological activity. Thus, the structure of the targeted enantiomerically pure N ‐(uracilylpentyl)‐β‐ D ‐ O ‐(5‐amino‐5‐deoxyribosyl)‐ L ‐serine retains uracil and 5‐amino‐5‐deoxyribose parts linked by a serinyl template. The synthetic strategy towards this compound relies on sequential O ‐glycosylation and N ‐alkylation by reductive amination of a serine derivative. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007)