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. 1979 Jan;137(1):644–647. doi: 10.1128/jb.137.1.644-647.1979

Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity.

M Matsuhashi, S Tamaki, S J Curtis, J L Strominger
PMCID: PMC218493  PMID: 368033

Abstract

The defect in D-alanine carboxypeptidase IA activity in the dacA11191 mutant of Escherichia coli was correlated with a defect in the release of penicillin G from penicillin-binding protein 5. The results suggest that penicillin-binding protein 5 catalyzes the major D-alanine carboxypeptidase IA activity of the wild type and that the mutation results in a defect in the deacylation step catalyzed by this enzyme.

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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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