Effect of cephapirin on formation of D-alanine carboxypeptidase in growing Bacillus subtilis cells.
Cephapirin was utilized to examine the interaction of beta-lactam antibiotics with growing Bacillus subtilis cells and the biological effects simultaneously produced. Saturation binding and quantitative cell death were observed at the cephapirin concentration of 0.1 mug/ml. Cephapirin bound to all penicillin-binding proteins except the d-alanine carboxypeptidase. A specific [(14)C]benzylpenicillin-binding assay was developed for the d-alanine carboxypeptidase. At the lowest saturating concentration of antibiotic (0.1 mug/ml), cephapirin inhibited formation of the d-alanine carboxypeptidase. Upon incubation with cephapirin, 18% of the membranous d-alanine carboxypeptidase was released into the media. The data suggest that beta-lactam antibiotics may affect the formation of bacterial cytoplasmic membranes in addition to their effect on cell wall synthesis.
D001412:Bacillus subtilis / Q000187:drug effects / Q000201:enzymology*; D001426:Bacterial Proteins / Q000032:analysis; D002268:Carboxypeptidases / Q000096:biosynthesis*; D002511:Cephalosporins / Q000494:pharmacology*; D002514:Cephapirin / Q000378:metabolism / Q000494:pharmacology*; D002267:Muramoylpentapeptide Carboxypeptidase / Q000096:biosynthesis*; D010400:Penicillin G / Q000378:metabolism; D013997:Time Factors
D001426:Bacterial Proteins; D002511:Cephalosporins; D002514:Cephapirin; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G