Squalamine and Aminosterol Mimics Inhibit the Peptidoglycan Glycosyltransferase Activity of PBP1b [PDF]
Antibiotics, 2020 Peptidoglycan (PG) is an essential polymer of the bacterial cell wall and a major antibacterial target. Its synthesis requires glycosyltransferase (GTase) and transpeptidase enzymes that, respectively, catalyze glycan chain elongation and their cross-linking to form the protective sacculus of the bacterial cell.
Adrien Boes +2 more
exaly +10 more sources
Peptidoglycan Glycosyltransferase Substrate Mimics as Templates for the Design of New Antibacterial Drugs [PDF]
Frontiers in Immunology, 2013 Peptidoglycan (PG) is an essential net-like macromolecule that surrounds bacteria, gives them their shape, and protects them against their own high osmotic pressure. PG synthesis inhibition leads to bacterial cell lysis, making it an important target for many antibiotics.
Adeline Derouaux +2 more
exaly +7 more sources
Rational structural modification of the isatin scaffold to develop new and potent antimicrobial agents targeting bacterial peptidoglycan glycosyltransferase [PDF]
RSC Advances, 2021 Isatin-based small molecules targeting bacterial peptidoglycan glycosyltransferase are potent antimicrobial agents againstS. aureus,E. coliand methicillin-resistantStaphylococcus aureusstrains.
Yong Wang, Siu-Cheong Yan, Pui-Kin So
exaly +6 more sources
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2007 Peptidoglycan is an essential polymer that forms a protective shell around bacterial cell membranes. Peptidoglycan biosynthesis is the target of many clinically used antibiotics, including the β-lactams, imipenems, cephalosporins, and glycopeptides.
Daniel Kähne +2 more
exaly +7 more sources
Importance of the Conserved Residues in the Peptidoglycan Glycosyltransferase Module of the Class A Penicillin-binding Protein 1b of Escherichia coli [PDF]
Journal of Biological Chemistry, 2008 The peptidoglycan glycosyltransferase (GT) module of class A penicillin-binding proteins (PBPs) and monofunctional GTs catalyze glycan chain elongation of the bacterial cell wall. These enzymes belong to the GT51 family, are characterized by five conserved motifs, and have some fold similarity with the phage lambda lysozyme.
Mohammed Terrak +2 more
exaly +8 more sources
Inactivation of the Monofunctional Peptidoglycan Glycosyltransferase SgtB Allows <i>Staphylococcus aureus</i> To Survive in the Absence of Lipoteichoic Acid. [PDF]
J Bacteriol, 2019 The bacterial cell wall acts as a primary defense against environmental insults such as changes in osmolarity. It is also a vulnerable structure, as defects in its synthesis can lead to growth arrest or cell death. The important human pathogen Staphylococcus aureus has a typical Gram-positive
Karinou E +4 more
europepmc +7 more sources
The Direction of Glycan Chain Elongation by Peptidoglycan Glycosyltransferases [PDF]
Journal of the American Chemical Society, 2007 Peptidoglycan glycosyltransferases (PGTs) are highly conserved enzymes that catalyze the polymerization of Lipid II to form the glycan strands of bacterial murein. Because they play a key role in bacterial cell wall synthesis, these enzymes are potentially important antibiotic targets; however, their mechanisms are not yet understood.
Deborah L, Perlstein +4 more
openaire +2 more sources
Analysis of Glycan Polymers Produced by Peptidoglycan Glycosyltransferases [PDF]
Journal of Biological Chemistry, 2007 Bacterial cells are surrounded by a cross-linked polymer called peptidoglycan, the integrity of which is necessary for cell survival. The carbohydrate chains that form the backbone of peptidoglycan are made by peptidoglycan glycosyltransferases (PGTs), highly conserved membrane-bound enzymes that are thought to be excellent targets for the development ...
Barrett, Dianah +5 more
openaire +4 more sources
Synthesis of Modified Peptidoglycan Precursor Analogues for the Inhibition of Glycosyltransferase [PDF]
Journal of the American Chemical Society, 2012 The peptidoglycan glycosyltransferases (GTs) are essential enzymes that catalyze the polymerization of glycan chains of the bacterial cell wall from lipid II and thus constitute a validated antibacterial target. Their enzymatic cavity is composed of a donor site for the growing glycan chain (where the inhibitor moenomycin binds) and an acceptor site ...
Dumbre, Shrinivas +6 more
openaire +3 more sources
Synthesis of Heptaprenyl−Lipid IV to Analyze Peptidoglycan Glycosyltransferases [PDF]
Journal of the American Chemical Society, 2007 Bacteria are surrounded by a cell wall containing layers of peptidoglycan, the integrity of which is essential for bacterial survival. In the final stage of peptidoglycan biosynthesis, peptidoglycan glycosyltransferases (PGTs; also known as transglycosylases) catalyze the polymerization of Lipid II to form linear glycan chains.
Yi, Zhang +5 more
openaire +2 more sources