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Antimicrob Agents Chemother. 1975 May; 7(5): 578-581
Copyright © 1975 American Society for Microbiology. All Rights Reserved.

DD-Carboxypeptidase and Peptidoglycan Transpeptidase from Pseudomonas aeruginosa

Pfizer Inc., Groton, Connecticut 06340

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 ß-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 ß-lactum antibiotic. This is in sharp contrast to the transpeptidase from Escherichia coli, which is sensitive to inhibition by penicillins and cephalosporins.

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