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. 1979 Jan;137(1):644-7.
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

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

M Matsuhashi et al. J Bacteriol. 1979 Jan.

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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References

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    1. J Biol Chem. 1978 Apr 25;253(8):2584-8 - PubMed
    1. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2631-5 - PubMed
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