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Open AccessJournal ArticleDOI

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

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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Journal ArticleDOI

Selective penicillin-binding protein imaging probes reveal substructure in bacterial cell division.

TL;DR: The designed and synthesized fluorescent and biotin derivatives of the β-lactam-containing antibiotic cephalosporin C probes represent new tools to explore a subset of PBPs and have the potential to facilitate a deeper understand of the roles of this critical class of proteins.
Journal ArticleDOI

Bacterial Enzymes and Antibiotic Resistance.

TL;DR: Analysis of the structure and functional characteristics of enzymes, which are the targets for different classes of antibiotics, will allow us to develop new strategies for overcoming the resistance.
Journal ArticleDOI

The Rcs stress response and accessory envelope proteins are required for de novo generation of cell shape in Escherichia coli

TL;DR: To regenerate normal morphology de novo, E. coli must supplement the classic FtsZ- and MreBCD-directed cell wall systems with activities that are otherwise dispensable for growth under normal laboratory conditions.
Journal ArticleDOI

Profiling of β-Lactam Selectivity for Penicillin-Binding Proteins in Streptococcus pneumoniae D39

TL;DR: In this paper, the authors evaluated 20 commercially available β-lactams for selective PBP inhibition in an unencapsulated derivative of the D39 strain of Streptococcus pneumoniae.
Journal ArticleDOI

Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome

TL;DR: Two mechanistically alternative strategies: ATP-dependent enzymes that generate acylphosphate intermediates and ATP-independent transacylation strategies are discussed, highlighting the function and synthetic utility of these amide bond-forming strategies.
References
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Book

Handbook of proteolytic enzymes

TL;DR: In this paper, Serine Peptidases with a Ser/Lys Catalytic Dyad (SC) are described, as well as their relation to the Nodavirus Coat Protein.

The Handbook of proteolytic enzymes

TL;DR: (Abbreviated Contents Including Section Headings:)
Journal ArticleDOI

Peptidoglycan structure and architecture

TL;DR: In several species examined, the fine structure of the peptidoglycan significantly varies with the growth conditions, and the different models for the architecture are discussed with respect to structural and physical parameters.
Journal ArticleDOI

Growth of the Stress-Bearing and Shape-Maintaining Murein Sacculus of Escherichia coli

TL;DR: A model is presented that postulates that maintenance of bacterial shape is achieved by the enzyme complex copying the preexisting murein sacculus that plays the role of a template.
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