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. 1977 Mar;74(3):1009–1012. doi: 10.1073/pnas.74.3.1009

Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.

N Georgopapadakou, S Hammarström, J L Strominger
PMCID: PMC430565  PMID: 403523

Abstract

The D-alanine carboxypeptidase of B. subtilis is a membrane-bound enzyme which is inhibited by penicillins and binds them covalently. The enzyme has been labeled with [14C]- or [35S]penicillin. After tryptic or Pronase digestion of the labeled, denatured, reduced, and carboxymethylated enzyme, a radioactive peptide was isolated in each case. The amino acid compositions of these two peptides are reported. The Pronase peptide was a subset of the tryptic peptide. Neither contained a cysteine residue and the only amino acid in the Pronase peptide to which the penicillin could be bound was a serine residue.

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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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