Effect of Cephapirin on Formation of d-Alanine Carboxypeptidase in Growing Bacillus subtilis Cells
AUTOR(ES)
White, John S.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=352633Documentos Relacionados
- d-Alanine Carboxypeptidase and Cell Wall Cross-Linking in Bacillus subtilis
- D-alanine incorporation into macromolecules and effects of D-alanine deprivation on active transport in Bacillus subtilis.
- Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.
- Inactivation of D-Alanine Carboxypeptidase by Penicillins and Cephalosporins Is Not Lethal in Bacillus subtilis
- Relation of Detergent HLB Number to Solubilization and Stabilization of D-Alanine Carboxypeptidase from Bacillus subtilis Membranes
