Skip to main content
Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1974 Dec;6(6):672–675. doi: 10.1128/aac.6.6.672

Penicillin-Resistant Mechanisms in Pseudomonas aeruginosa: Effects of Penicillin G and Carbenicillin on Transpeptidase and d-Alanine Carboxypeptidase Activities

Hidekazu Suginaka 1, Akira Ichikawa 1, Shozo Kotani 1
PMCID: PMC444717  PMID: 4217580

Abstract

A membrane fraction from Pseudomonas aeruginosa KM 338 was shown to catalyze in vitro peptidoglycan synthesis from uridine 5′-diphosphate-N-acetylmuramyl-l-alanyl-d- glutamyl-meso-diaminopimelyl-d-alanyl-d-alanine and uridine 5′-diphosphate-N-acetylglucosamine. Synthesized peptidoglycan was partially cross-linked by transpeptidation, which was accompanied by the release of d-alanine. This reaction was strongly inhibited by 25 and 50 μg of penicillin G and carbenicillin per ml respectively, whereas the intact cells were relatively resistant to penicillins (minimal inhibitory concentration of penicillin G and carbenicillin, 30 and 0.125 mg/ml, respectively). Soluble d-alanine carboxypeptidase present in P. aeruginosa KM 338 was studied as well, which was found almost completely inhibited by penicillin G and carbenicillin (10 μg/ml).

Full text

PDF
675

Selected References

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

  1. Araki Y., Shimada A., Ito E. Effect of penicillin on cell wall mucopeptide synthesis in a Escherichia coli particulate system. Biochem Biophys Res Commun. 1966 May 25;23(4):518–525. doi: 10.1016/0006-291x(66)90760-1. [DOI] [PubMed] [Google Scholar]
  2. Heilmann H. D. On the peptidoglycan of the cell walls of Pseudomonas aeruginosa. Eur J Biochem. 1972 Dec 18;31(3):456–463. doi: 10.1111/j.1432-1033.1972.tb02552.x. [DOI] [PubMed] [Google Scholar]
  3. Izaki K., Matsuhashi M., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. 8. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli. J Biol Chem. 1968 Jun 10;243(11):3180–3192. [PubMed] [Google Scholar]
  4. Izaki K., Matsuhashi M., Strominger J. L. Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. Proc Natl Acad Sci U S A. 1966 Mar;55(3):656–663. doi: 10.1073/pnas.55.3.656. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Izaki K., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli. J Biol Chem. 1968 Jun 10;243(11):3193–3201. [PubMed] [Google Scholar]
  6. LEDERBERG J. Mechanism of action of penicillin. J Bacteriol. 1957 Jan;73(1):144–144. doi: 10.1128/jb.73.1.144-144.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lawrence P. J., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. XVI. The reversible fixation of radioactive penicillin G to the D-alanine carboxypeptidase of Bacillus subtilis. J Biol Chem. 1970 Jul 25;245(14):3660–3666. [PubMed] [Google Scholar]
  8. Lederberg J. BACTERIAL PROTOPLASTS INDUCED BY PENICILLIN. Proc Natl Acad Sci U S A. 1956 Sep;42(9):574–577. doi: 10.1073/pnas.42.9.574. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Martin H. H., Heilmann H. D., Preusser H. J. State of the rigid-layer in celll walls of some gram-negative Bacteria. Arch Mikrobiol. 1972;83(4):332–346. doi: 10.1007/BF00425246. [DOI] [PubMed] [Google Scholar]
  10. Mirelman D., Sharon N. Biosynthesis of peptidoglycan by a cell wall preparation of Staphylococcus aureus and its inhibition by penicillin. Biochem Biophys Res Commun. 1972 Mar 10;46(5):1909–1917. doi: 10.1016/0006-291x(72)90069-1. [DOI] [PubMed] [Google Scholar]
  11. PARK J. T., STROMINGER J. L. Mode of action of penicillin. Science. 1957 Jan 18;125(3238):99–101. doi: 10.1126/science.125.3238.99. [DOI] [PubMed] [Google Scholar]
  12. PARK J. T. Uridine-5'-pyrophosphate derivatives. II. Isolation from Staphylococcus aureus. J Biol Chem. 1952 Feb;194(2):877–884. [PubMed] [Google Scholar]
  13. STROMINGER J. L., PARK J. T., THOMPSON R. E. Composition of the cell wall of Staphylococcus aureus: its relation to the mechanism of action of penicillin. J Biol Chem. 1959 Dec;234:3263–3268. [PubMed] [Google Scholar]
  14. Schleifer K. H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev. 1972 Dec;36(4):407–477. doi: 10.1128/br.36.4.407-477.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Strominger J. L., Blumberg P. M., Suginaka H., Umbreit J., Wickus G. G. How penicillin kills bacteria: progress and problems. Proc R Soc Lond B Biol Sci. 1971 Dec 31;179(1057):369–383. doi: 10.1098/rspb.1971.0103. [DOI] [PubMed] [Google Scholar]
  16. Suginaka H., Blumberg P. M., Strominger J. L. Multiple penicillin-binding components in Bacillus subtilis, Bacillus cereus, Staphylococcus aureus, and Escherichia coli. J Biol Chem. 1972 Sep 10;247(17):5279–5288. [PubMed] [Google Scholar]
  17. Tipper D. J., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. XII. Inhibition of cross-linking by penicillins and cephalosporins: studies in Staphylococcus aureus in vivo. J Biol Chem. 1968 Jun 10;243(11):3169–3179. [PubMed] [Google Scholar]
  18. 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]
  19. 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]

Articles from Antimicrobial Agents and Chemotherapy are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES