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. 1973 Feb;3(2):181–187. doi: 10.1128/aac.3.2.181

dd-Carboxypeptidase-Transpeptidase and Killing Site of β-Lactam Antibiotics in Streptomyces Strains R39, R61, and K11

Jean Dusart 1,2,3, Alberto Marquet 1,2,3, Jean-Marie Ghuysen 1,2,3, Jean-Marie Frère 1,2,3, Ramon Moreno 1,2,3, Melina Leyh-Bouille 1,2,3, Kenneth Johnson 1,2,3,1, Chantal Lucchi 1,2,3, Harold R Perkins 1,2,3, Manuel Nieto 1,2,3
PMCID: PMC444384  PMID: 4790585

Abstract

Additional evidence is given that in Streptomyces strains R39, R61, and K11 the same enzyme performs dd-carboxypeptidase and transpeptidase activities and that this enzyme is the killing site of β-lactam antibiotics. With strain R61, it was found that the exocellular enzyme has a sensitivity towards some antibiotics different from that of the membrane-bound enzyme. Under the growth conditions used in the present investigations, β-lactamase activity was not involved in susceptibility to β-lactam antibiotics.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blumberg P. M., Strominger J. L. Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2814–2817. doi: 10.1073/pnas.68.11.2814. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. FOLEY J. M., PERRET C. J. Screening bacterial colonies for penicillinase production. Nature. 1962 Jul 21;195:287–288. doi: 10.1038/195287a0. [DOI] [PubMed] [Google Scholar]
  3. GHUYSEN J. M. Activités bactériolytiques de l'actinomycetine de Streptomyces albus G. Arch Int Physiol Biochim. 1957 Apr;65(2):173–305. [PubMed] [Google Scholar]
  4. Johnson K., Dusart J., Campbell J. N., Ghuysen J. M. Exocellular beta-lactamases of Streptomyces albus G and strains R39 and K11. Antimicrob Agents Chemother. 1973 Feb;3(2):289–298. doi: 10.1128/aac.3.2.289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Leyh-Bouille M., Coyette J., Ghuysen J. M., Idczak J., Perkins H. R., Nieto M. Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61. Biochemistry. 1971 May 25;10(11):2163–2170. doi: 10.1021/bi00787a032. [DOI] [PubMed] [Google Scholar]
  6. Leyh-Bouille M., Nakel M., Frère J. M., Johnson K., Ghuysen J. M., Nieto M., Perkins H. R. Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11. Biochemistry. 1972 Mar 28;11(7):1290–1298. doi: 10.1021/bi00757a027. [DOI] [PubMed] [Google Scholar]
  7. Muñoz E., Marquet A., Larraga V., Coyette J. Isolation, partial characterization of the cytoplasmic membrane fraction of Streptomyces albus G and DD-carboxypeptidase localization. Arch Mikrobiol. 1972;81(3):273–288. doi: 10.1007/BF00412246. [DOI] [PubMed] [Google Scholar]
  8. Pollock J. J., Ghuysen J. M., Linder R., Salton M. R., Perkins H. R., Nieto M., Leyh-Bouille M., Frere J. M., Johnson K. Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases. Proc Natl Acad Sci U S A. 1972 Mar;69(3):662–666. doi: 10.1073/pnas.69.3.662. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Rogers H. J. The inhibition of mucopeptide synthesis by benzylpenicillin in relation to irreversible fixation of the antibiotic by staphylococci. Biochem J. 1967 Apr;103(1):90–102. doi: 10.1042/bj1030090. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Saz A. K. An introspective view of penicillinase. J Cell Physiol. 1970 Dec;76(3):397–403. doi: 10.1002/jcp.1040760318. [DOI] [PubMed] [Google Scholar]
  11. Tipper D. J., Strominger J. L. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1133–1141. doi: 10.1073/pnas.54.4.1133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Wise E. M., Jr, Park J. T. Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis. Proc Natl Acad Sci U S A. 1965 Jul;54(1):75–81. doi: 10.1073/pnas.54.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]

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