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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Nov;68(11):2814–2817. doi: 10.1073/pnas.68.11.2814

Inactivation of D-Alanine Carboxypeptidase by Penicillins and Cephalosporins Is Not Lethal in Bacillus subtilis

Peter M Blumberg 1, Jack L Strominger 1
PMCID: PMC389532  PMID: 4330943

Abstract

The D-alanine carboxypeptidase of Bacillus subtilis is a particulate enzyme that is irreversibly inactivated by penicillins and cephalosporins. However, the lethal concentrations of these antibiotics are not the same as those that inhibit enzymatic activity in vitro. 6-Aminopenicillanic acid inactivates at least 95% of the enzyme at nonlethal concentrations. Conversely, cephalothin is lethal at concentrations that do not inactivate the enzyme. Experiments with intact, growing cells confirm the results obtained in vitro. Therefore, a killing site distinct from the carboxypeptidase must be postulated.

Keywords: peptidoglycan, mucopeptide, cell wall, 6-aminopenicillanic acid, cephalothin, cloxacillin

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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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