Journal of Bacteriology, July 2008, p. 4782-4785, Vol. 190, No. 13
0021-9193/08/$08.00+0 doi:10.1128/JB.00025-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Lionel Dubost,4
Arul Marie,4
Michel Arthur,1,2,3 and
Laurent Gutmann1,2,3,5*
INSERM, U872, LRMA, Centre de Recherche des Cordeliers, Equipe 12, Paris, F-75006 France,1 Université Pierre et Marie Curie-Paris 6, UMR S 872, Paris F-75006, France,2 Université Paris Descartes, UMR S 872, Paris F-75006, France,3 Muséum National d'Histoire Naturelle, Plateforme de Spectrométrie de Masse et de Protéomique, Paris, France,4 AP-HP, Hôpital Européen Georges Pompidou, Paris, F-75015 France5
Received 5 January 2008/ Accepted 23 April 2008
Three active-site cysteine L,D-transpeptidases can individually anchor the Braun lipoprotein to the Escherichia coli peptidoglycan. We show here that two additional enzymes of the same family form peptide bonds between the third residues of peptidoglycan stems, generating meso-DAP3
meso-DAP3 unusual cross-links. This activity partially replaces the D,D-transpeptidase activity of penicillin-binding proteins.
Published ahead of print on 2 May 2008.
Present address: Ecole Polytechnique Fédérale de Lausanne, Sciences de la Vie, Lausanne, Switzerland.
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