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.read more
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References
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TL;DR: It is proposed that the Actinomadura R39 PBP and E. coli PBP4 form a special class, class C, of low-Mr PBPs/DD-peptidases, and the 174-amino-acid insert occurs at equivalent places in the two PBPs, away from the active site.
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Listeria monocytogenes EGD lacking penicillin‐binding protein 5 (PBP5) produces a thicker cell wall
TL;DR: Purified PBP5 has dd-carboxypeptidase activity, removing the terminal D-alanine residue from murein pentapeptide side chains, and shows higher activity against low molecular weight monomeric pentAPEptide substrates compared to dimeric pentapePTide compound.
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TL;DR: The presence of highly divergent mosaic blocks in penicillin binding protein genes responsible for Penicillin resistance in Streptococcus pneumoniae implies that transformation is an important tool for the evolution of this pathogen.
Journal ArticleDOI
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