Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-γ-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase

RL Harding, J Henshaw, J Tilling…

Index: Harding, Ross L.; Henshaw, Joanne; Tilling, Joannah; Bugg, Timothy D.H. Journal of the Chemical Society. Perkin Transactions 1, 2002 , # 14 p. 1714 - 1722

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Citation Number: 6

Abstract

MurNAc-L-amidase is one of a family of peptidoglycan hydrolases which catalyses the breakdown of bacterial peptidoglycan. Analogues of the peptidoglycan fragment MurNAc-L- Ala-γ-D-Glu containing S-thiolactic acid in place of L-alanine were synthesised as thioester substrates for this enzyme. Triphenylmethanethiol was used to develop a stereoselective synthesis of S-thiolactic acid, which was elaborated synthetically into MurNAc-dipeptide ...