Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-gamma-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase
UNSPECIFIED. (2002) Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-gamma-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1 (14). pp. 1714-1722. ISSN 1472-7781Full text not available from this repository.
Official URL: http://dx.doi.org/10.1039/b200921h
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-gamma-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-gamma-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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1|
|Publisher:||ROYAL SOC CHEMISTRY|
|Number of Pages:||9|
|Page Range:||pp. 1714-1722|
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