Penicillin-Resistant Mechanisms in Pseudomonas aeruginosa : Effects of Penicillin G and Carbenicillin on Transpeptidase and d -Alanine Carboxypeptidase Activities
- 1 December 1974
- journal article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 6 (6) , 672-675
- https://doi.org/10.1128/aac.6.6.672
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).Keywords
This publication has 18 references indexed in Scilit:
- On the Peptidoglycan of the Cell Walls of Pseudomonas aeruginosaEuropean Journal of Biochemistry, 1972
- Biosynthesis of peptidoglycan by a cell wall preparation of Staphylococcus aureus and its inhibition by penicillinBiochemical and Biophysical Research Communications, 1972
- How penicillin kills bacteria: progress and problemsProceedings of the Royal Society of London. B. Biological Sciences, 1971
- Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli.1968
- BIOSYNTHESIS OF PEPTIDOGLYCAN OF BACTERIAL CELL WALLS .12. INHIBITION OF CROSS-LINKING BY PENICILLINS AND CEPHALOSPORINS - STUDIES IN STAPHYLOCOCCUS AUREUS IN VIVO1968
- BIOSYNTHESIS OF PEPTIDOGLYCAN OF BACTERIAL CELL WALLS .13. PEPTIDOGLYCAN TRANSPEPTIDASE AND D-ALANINE CARBOXYPEPTIDASE - PENICILLIN-SENSITIVE ENZYMATIC REACTION IN STRAINS OF ESCHERICHIA COLI1968
- Effect of penicillin on cell wall mucopeptide synthesis in a Escherichia coli particulate systemBiochemical and Biophysical Research Communications, 1966
- Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions.Proceedings of the National Academy of Sciences, 1966
- Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.Proceedings of the National Academy of Sciences, 1965
- Mode of Action of PenicillinScience, 1957