dd -Carboxypeptidase and Peptidoglycan Transpeptidase from Pseudomonas aeruginosa
Open Access
- 1 May 1975
- journal article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 7 (5) , 578-581
- https://doi.org/10.1128/aac.7.5.578
Abstract
Peptidoglycan transpeptidase and dd -carboxypeptidase have been detected in isolated membranes of Pseudomonas aeruginosa . Cephalosporins and penicillins fail to inhibit the transpeptidase at concentrations as high as 100 μg/ml. dd -Carboxypeptidase, on the other hand, is sensitive to inhibition by β-lactam antibiotics. The presence of dimethyl sulfoxide in the reaction mixture results in a twofold stimulation of peptidoglycan formation, whereas dd -carboxypeptidase is inhibited approximately 30%. Maximum stimulation of transpeptidase occurs in the presence of both dimethyl sulfoxide and a β-lactum antibiotic. This is in sharp contrast to the transpeptidase from Escherichia coli , which is sensitive to inhibition by penicillins and cephalosporins.Keywords
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