Advertisement

Penicillin-Binding Proteins of Bacteria

  • John W. Kozarich
  • Christine E. Buchanan
  • Susan J. Curtis
  • Sven Hammarström
  • Jack L. Strominger
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 84)

Abstract

The penicillin-binding components of bacteria are presumably enzymes of cell wall peptidoglycan synthesis, and one or more of these is a presumed killing site for penicillins. All organisms which have so far been examined contain multiple penicillin-binding components, e.g., there are five in Bacillus subtilis, six in Escherichia coli, and four in Staphylococcus aureus. Progress in studying these components includes: 1) The demonstration that the hydroxylamine-induced release of penicillin G from several penicillin-binding components is enzymatically catalyzed. In addition, the effect of sulfhydryl reagents on the catalytic and penicillin binding activities of E. coli carboxypeptidase IA suggests that a thiol group is involved in a deacylation reaction of the enzyme. 2) One of the S. aureus binding components can be isolated by affinity chromatography based on the reversibility of its penicillin binding. Under appropriate conditions it can catalyze transpeptidase, carboxypeptidase and penicillinase activities. 3) Altered penicillin-binding components are found in mutants of B. subtilis which have been isolated as step-wise penicillin-resistant organisms, 4) The penicilloyl residue of the penicillin-binding components is released at a slow rate in a novel, enzymatically catalyzed degradation. The products of this degradation in the case of the B. stearothermophilus D-alanine carboxypeptidase have been identified as phenylacetylglycine and 5,5-dimethylthiazoline carboxylic acid.

Keywords

Thiol Group Penicillin Resistance Killing Site Carboxypeptidase Activity Bacterial Cell Wall Synthesis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Anderson, B.M., Cordes, E.H., and Jencks, W.P.: J. Biol. Chem. 236 (1961) 455.PubMedGoogle Scholar
  2. 2.
    Bell, M.R., Carlson, J.A. and Oesterlin, R.: J. Org. Chem. 37 (1972) 2733.PubMedCrossRefGoogle Scholar
  3. 3.
    Blumberg, P.M. and Strominger, J.L.: Proc. Nat. Acad. Sci. USA 68 (1971) 2814.PubMedCrossRefGoogle Scholar
  4. 4.
    Blumberg, P.M. and Strominger, J.L.: Proc. Nat. Acad. Sci. USA 69 (1972) 3751.PubMedCrossRefGoogle Scholar
  5. 5.
    Blumberg, P.M. and Strominger, J.L.: J. Biol. Chem. 247 (1972) 8107.PubMedGoogle Scholar
  6. 6.
    Blumberg, P.M. and Strominger, J.L.: Bacteriol. Rev. 38 (1974) 291.PubMedGoogle Scholar
  7. 7.
    Blumberg, P.M. and Strominger, J.L.: Methods Enzymol. 34 (1974) 401.PubMedCrossRefGoogle Scholar
  8. 8.
    Blumberg, P.M., Yocum, R.R., Willoughby, E., and Strominger, J.L.: J. Biol. Chem. 249 (1974) 6828.PubMedGoogle Scholar
  9. 9.
    Buchanan, C.E. and Strominger, J.L.: Proc. Nat. Acad. Sci. USA in press.Google Scholar
  10. 10.
    Demerec, M.: J. Bacteriol. 56 (1948) 63.Google Scholar
  11. 11.
    Dixon, G.H., Dreyer, W.J., and Neurath, H.: J. Amer. Chem. Soc. 78 (1956) 4810.CrossRefGoogle Scholar
  12. 12.
    Ghuysen, J.M. et. al: Bulletin De L’Institut Pasteur 73 (1975) 101.Google Scholar
  13. 13.
    Hammarstrom, S. and Strominger, J.L.: Proc. Nat. Acad. Sci. USA 72 (1975) 3463.PubMedCrossRefGoogle Scholar
  14. 14.
    Hammarstrom, S. and Strominger, J.L.: submitted for publication.Google Scholar
  15. 15.
    Kozarich, J.W. and Strominger, J.L.: submitted for publication.Google Scholar
  16. 16.
    Kozarich, J.W., Willoughby, E., and Strominger, J.L.: submitted for publication.Google Scholar
  17. 17.
    Lawrence, P.J. and Strominger, J.L.: J. Biol. Chem. 245 (1970) 3653.PubMedGoogle Scholar
  18. 18.
    Lawrence, P.J. and Strominger, J.L.: J. Biol. Chem. 245 (1970) 3660.PubMedGoogle Scholar
  19. 19.
    Mirelman, D. and Sharon, N.: Biochem. Biophys. Res. Commun. 46 (1972) 1909.PubMedCrossRefGoogle Scholar
  20. 20.
    Spratt, B.G. and Pardee, A.B.: Nature 254 (1975) 516.PubMedCrossRefGoogle Scholar
  21. 21.
    Spratt, B.G. and Strominger, J.L.: submitted for publication.Google Scholar
  22. 22.
    Strominger, J.L., Willoughby, E., Kamiryo, T., Blumberg, P.M. and Yocum, R.R.: Ann. N.Y. Acad. Sci. 235 (1974) 210.PubMedCrossRefGoogle Scholar
  23. 23.
    Tamura, T., Imae, Y., and Strominger, J.L. J. Biol. Chem. 251 (1976) 414.Google Scholar
  24. 24.
    Tipper, D.J. and Strominger, J.L.: Proc. Nat. Acad. Sci USA 54 (1965) 1133.PubMedCrossRefGoogle Scholar
  25. 25.
    Yocum, R.R., Blumberg, P.M., and Strominger, J.L.: J. Biol. Chem. 249 (1974) 4863.PubMedGoogle Scholar
  26. 26.
    Frere, J-M., et al. Nature 260 (1976) 451–454.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • John W. Kozarich
    • 1
  • Christine E. Buchanan
    • 1
  • Susan J. Curtis
    • 1
  • Sven Hammarström
    • 1
  • Jack L. Strominger
    • 1
  1. 1.The Biological LaboratoriesHarvard UniversityCambridgeUSA

Personalised recommendations