Abstract
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.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Chromatography, High Pressure Liquid
-
Escherichia coli / enzymology
-
Escherichia coli / genetics
-
Escherichia coli / metabolism*
-
Escherichia coli Proteins / genetics
-
Escherichia coli Proteins / metabolism*
-
Models, Chemical
-
Penicillin-Binding Proteins / genetics
-
Penicillin-Binding Proteins / metabolism
-
Peptidoglycan / chemistry
-
Peptidoglycan / metabolism
-
Peptidyl Transferases / genetics
-
Peptidyl Transferases / metabolism*
Substances
-
Escherichia coli Proteins
-
Penicillin-Binding Proteins
-
Peptidoglycan
-
Peptidyl Transferases