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. 1979 Feb;15(2):204–208. doi: 10.1128/aac.15.2.204

Effect of Cephapirin on Formation of d-Alanine Carboxypeptidase in Growing Bacillus subtilis Cells

John S White 1,†, Mark Astill 1,‡, Paul J Lawrence 1,§
PMCID: PMC352633  PMID: 106774

Abstract

Cephapirin was utilized to examine the interaction of β-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 μg/ml. Cephapirin bound to all penicillin-binding proteins except the d-alanine carboxypeptidase. A specific [14C]benzylpenicillin-binding assay was developed for the d-alanine carboxypeptidase. At the lowest saturating concentration of antibiotic (0.1 μg/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 β-lactam antibiotics may affect the formation of bacterial cytoplasmic membranes in addition to their effect on cell wall synthesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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