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

Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-gamma-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase
Thioester analogues of peptidoglycan fragment MurNAc-L-Ala-gamma-D-Glu as substrates for peptidoglycan hydrolase MurNAc-L-Ala amidase
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.
l-alanine amidase, cell-wall hydrolases, acid, cloning, enzymes
1714-1722
Harding, R. L.
27c5b543-f404-4ac9-80f4-80799b9e56a1
Henshaw, J.
07e5922f-b420-4223-9c12-3066d54a3d37
Tilling, J.
1031405a-9bae-497a-92e9-f688dc2df078
Bugg, T. D. H.
a1d6d985-d7ba-408d-a4d1-9bfa0c0642bf
Harding, R. L.
27c5b543-f404-4ac9-80f4-80799b9e56a1
Henshaw, J.
07e5922f-b420-4223-9c12-3066d54a3d37
Tilling, J.
1031405a-9bae-497a-92e9-f688dc2df078
Bugg, T. D. H.
a1d6d985-d7ba-408d-a4d1-9bfa0c0642bf

Harding, R. L., Henshaw, J., Tilling, J. and Bugg, T. D. H. (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), 1714-1722. (doi:10.1039/b200921h).

Record type: Article

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-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.

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More information

Published date: 2002
Keywords: l-alanine amidase, cell-wall hydrolases, acid, cloning, enzymes

Identifiers

Local EPrints ID: 19757
URI: http://eprints.soton.ac.uk/id/eprint/19757
PURE UUID: 2553eeed-e767-4883-bce1-8e4e1edc363a

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Date deposited: 20 Feb 2006
Last modified: 08 Jan 2022 00:59

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Contributors

Author: R. L. Harding
Author: J. Henshaw
Author: J. Tilling
Author: T. D. H. Bugg

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