title: Peptidoglycan transpeptidase inhibition in Pseudomonas aeruginosa and Escherichia coli by Penicillins and Cephalosporins.
abstract: Peptidoglycan transpeptidase activity has been studied in cells of Escherichia coli 146 and Pseudomonas aeruginosa 56 made permeable to exogenous, nucleotide-sugar peptidoglycan precursors by ether treatment. Transpeptidase activity was inhibited, in both organisms, by a range of penicillins and cephalosporins, the Pseudomonas enzyme being more sensitive to inhibition in each case. Conversely, growth of E. coli 146 was more susceptible to these antibiotics than growth of P. aeruginosa 56. Furthermore, similar transpeptidase inhibition values were ob-obtained for the four penicillins examined against the Pseudomonas enzyme, although only two of these (carbenicillin and pirbenicillin) inhibited the growth of this organism. We therefore conclude that the high resistance of P. aeruginosa 56 to growth inhibition by most beta-lactam antibiotics cannot be due to an insensitive peptidoglycan transpeptidase.
mesh_terms: D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D019881:Aminoacyltransferases; D002511:Cephalosporins / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D008826:Microbial Sensitivity Tests; D010406:Penicillins / Q000494:pharmacology*; D010457:Peptidoglycan; D010458:Peptidyl Transferases / Q000037:antagonists & inhibitors*; D011550:Pseudomonas aeruginosa / Q000187:drug effects / Q000201:enzymology*
chemical_list: D002511:Cephalosporins; D010406:Penicillins; D010457:Peptidoglycan; D000217:Acyltransferases; D019881:Aminoacyltransferases; C022330:peptidoglycan transpeptidase; D010458:Peptidyl Transferases