Topic
Penicillin binding
About: Penicillin binding is a research topic. Over the lifetime, 158 publications have been published within this topic receiving 6017 citations.
Papers published on a yearly basis
Papers
TL;DR: An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.
Abstract: Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria. This review focuses on the detailed structure of PBPs and their implication in peptidoglycan synthesis, maturation and recycling. An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.
1,277 citations
TL;DR: The identification of a minor penicillin binding protein is reported which is believed to be the target at which the amidinopenicillanic acid designated FL1060 acts to affect the shape of Escherichia coli.
Abstract: β-LACTAM antibiotics (penicillins and cephalosporins) have attracted considerable attention as probes of cell growth and division1,2. Although extensive studies have been made on both penicillin-sensitive enzymes and penicillin binding proteins3, there has been no clear indication of the role of any of these components in the effects of β-lactam antibiotics on cell growth. We report the identification of a minor penicillin binding protein which we believe to be the target at which the amidinopenicillanic acid designated FL1060 (ref. 4) acts to affect the shape of Escherichia coli. This is the first example of the identification of a penicillin binding protein with an essential and defined role in bacterial cell growth.
395 citations
TL;DR: The construction of an isogenic set of transformants with increasing levels of penicillin resistance indicated that the penA gene was associated with a decrease inPenicillin binding fo PBP 2, and decreased binding to PBP 1 is likely to accompany the newly reported pem and tem genes, which govern to highest level of peniillin resistance.
Abstract: The penicillin-binding proteins (PBPs) of Neisseria gonorrhoeae were investigated by using [3H]benzylpenicillin of high specific activity. This made it possible to label the PBPs both in cytoplasmic membranes and in the membranes of actively growing cells (in vivo labeling). A total of 20 strains isolated from different geographic locales showed the same pattern of three major PBPs, which had molecular weights of approximately 90,000, 63,000, and 48,000. Five clinical isolates of intrinsically penicillin-resistant gonococci each exhibited reduced penicillin binding of PBPs 1 and 2. The construction of an isogenic set of transformants with increasing levels of penicillin resistance indicated that the penA gene was associated with a decrease in penicillin binding fo PBP 2. Decreased binding to PBP 1 is likely to accompany the newly reported pem and tem genes, which govern to highest level of penicillin resistance.
148 citations
TL;DR: The exocellular DD-carboxypeptidases-transpeptidase that is excreted by Streptomyces R61 during growth, is very sensitive to penicillin and appears to be a good model for the study of the interaction between the enzyme, substrates and antibiotic.
114 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 5 |
| 2020 | 1 |
| 2019 | 7 |
| 2018 | 1 |
| 2017 | 1 |
| 2016 | 5 |