scispace - formally typeset
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.

read more

Citations
More filters
Dissertation

Directed evolution of penicillin V acylase from "Streptomyces lavendulae" and aculeacin A acylase from "Actinoplanes utahensis"

TL;DR: AuAAC (Au-Homoserin lactona acilasa) putativa as discussed by the authors ) is a putativization of A. utahensis.
Book ChapterDOI

Resistance of Gram-Negative Bacilli to Antimicrobials

TL;DR: This chapter discusses antibiotic resistance in Gram-negative pathogens, beginning with the intrinsic resistance engendered by their unique outer membrane combined with active efflux and extending to the broad range of mechanisms including upregulation of efflux, alterations of cell envelope, mutation of antibacterial target genes, antibiotic-modifying enzymes, and target-protection mechanisms that are found in this diverse group of organisms.
Journal ArticleDOI

The bla and mec families of β-lactam resistance genes in the genera Macrococcus, Mammaliicoccus and Staphylococcus: an in-depth analysis with emphasis on Macrococcus.

TL;DR: Macrococcus is revealed as an important source for mobilization of antibiotic resistance genes within the family of Staphylococcaceae, revealing the different recombinases and integrases that contribute to the mobility of methicillin resistance genes.
References
More filters
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.
Related Papers (5)