Identification of the L,D-transpeptidases for peptidoglycan cross-linking in Escherichia coli.
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-DAP(3)-->meso-DAP(3) unusual cross-links. This activity partially replaces the D,D-transpeptidase activity of penicillin-binding proteins.
Magnet
Sophie
S
INSERM U872-LRMA, Equipe 12, Centre de Recherche des Cordeliers, 15 Rue de l'Ecole de Médecine, 75270 Paris, Cedex 06, France.
Dubost
Lionel
L
Marie
Arul
A
Arthur
Michel
M
Gutmann
Laurent
L
D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D008956:Models, Chemical; D046915:Penicillin-Binding Proteins / Q000235:genetics / Q000378:metabolism; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism; D010458:Peptidyl Transferases / Q000235:genetics / Q000378:metabolism*
D029968:Escherichia coli Proteins; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan; D010458:Peptidyl Transferases