276682-02-1Relevant articles and documents
Use of trityl thiol for stereoselective thioester synthesis: A new preparation of (S)-thiolactic acid
Harding, Ross L.,Bugg, Timothy D. H.
, p. 2729 - 2731 (2000)
Trityl thiol is found to be a convenient reagent for the enantioselective preparation of (S)-thiolactic acid and a muramic acid thioester. (C) 2000 Elsevier Science Ltd.
Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-γ-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase
Harding, Ross L.,Henshaw, Joanne,Tilling, Joannah,Bugg, Timothy D.H.
, p. 1714 - 1722 (2007/10/03)
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 analogues. MurNAc-S-thioacetyl-N-propylamide 13 and MurNAc-S-thiolactyl-2R-alaninamide 16 were found not to be substrates for recombinant MurNAc-L-Ala amidases CwlA from Bacillus subtilis and Ply21 from bacteriophage TP21, however, turnover of tripeptide thioester S-propionylthiolactyl-γ-D-Glu-L-Lys-OMe 21 was observed using amidase Ply21. Therefore, recognition of the amino acid at position 3 of the pentapeptide sidechain appears to be important for enzymatic turnover.