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The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

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TLDR
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.

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The Bacterial Cell Envelope

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The oyster genome reveals stress adaptation and complexity of shell formation

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Three Decades of β-Lactamase Inhibitors

TL;DR: In this paper, the authors review the catalytic mechanisms of each β-lactamase class and discuss approaches for circumventing β-latamase-mediated resistance, including properties and characteristics of mechanism-based inactivators.
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Bacterial peptidoglycan (murein) hydrolases.

TL;DR: The current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase is reviewed.
References
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Penicillin binding proteins in Listeria monocytogenes.

TL;DR: The amount of antibiotic concentration preventing an effective label by the radioactive probe to the detected penicillin binding proteins seems to correlate with the lethal concentration of the different antibiotics on Listeria monocytogenes and explains the natural resistance of this genus to certain beta-lactamic compounds.
Journal ArticleDOI

Identification and characterization of a conserved outer-membrane protein of Neisseria gonorrhoeae.

TL;DR: Results are reported which confirm that the 44 kDa protein is surface‐exposed, and that the protein is expressed in, and is structurally invariant among, 14 strains of N. gonorrhoeae.
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The d-Methyl Group in β-Lactamase Evolution: Evidence from the Y221G and GC1 Mutants of the Class C β-Lactamase of Enterobacter cloacae P99†

TL;DR: The serine β-lactamases are evolutionary descendants of dd-peptidases and retain much of their structure, particularly at the active site, and differ in being able to catalyze hydrolysis of acyl-enzyme intermediates derived from β- lactams and being unable to efficiently catalyze acyl transfer reactions of d-alanyl-d-alanine terminating peptides.
Journal Article

Analysis of the murein of a Listeria monocytogenes EGD mutant lacking functional penicillin binding protein 5 (PBP5).

TL;DR: Cells of a mutant of Listeria monocytogenes lacking functional PBP5, an enzyme with DD-carboxypeptidase activity, make thicker cells walls, showing a shift in profile from less cross-linked muropeptides (monomers, dimers) towards more highly cross- linked ones.
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