Results 41 to 50 of about 2,643 (172)
The mechanistic landscape of Lytic transglycosylase as targets for antibacterial therapy
Lytic transglycosylases (Ltgs) are glycan strand cleaving enzymes whose role is poorly understood in the genesis of the bacterial envelope. They play multiple roles in all stages of a bacterial life cycle, by creating holes in the peptidoglycan that is necessary for cell division and separation.
Elizabeth A. Martinez-Bond +2 more
openaire +2 more sources
Peptidoglycan, found within the cell wall of bacteria, is a structure critical for maintaining cell morphology and providing a protective barrier in diverse environments. Peptidoglycan is a remarkably dynamic structure that is constantly remodeled during
Beth A. Bachert, Joel A. Bozue
doaj +1 more source
Lytic transglycosylases: concinnity in concision of the bacterial cell wall [PDF]
The lytic transglycosylases (LTs) are bacterial enzymes that catalyze the non-hydrolytic cleavage of the peptidoglycan structures of the bacterial cell wall. They are not catalysts of glycan synthesis as might be surmised from their name. Notwithstanding the seemingly mundane reaction catalyzed by the LTs, their lytic reactions serve bacteria for a ...
David A. Dik +3 more
openaire +2 more sources
Correction for Wang et al., “An inhibitor/anti-inhibitor system controls the activity of lytic transglycosylase MltF in Pseudomonas aeruginosa” [PDF]
Michelle Wang +2 more
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Antibiotic Targets in Gonococcal Cell Wall Metabolism
The peptidoglycan cell wall that encloses the bacterial cell and provides structural support and protection is remodeled by multiple enzymes that synthesize and cleave the polymer during growth.
Krizia M. Pérez Medina +1 more
doaj +1 more source
Lytic transglycosylases: Bacterial space-making autolysins
Lytic transglycosylases are an important class of bacterial enzymes that act on peptidoglycan with the same substrate specificity as lysozyme. Unlike the latter enzymes, however, the lytic transglycosylases are not hydrolases but instead cleave the glycosidic linkage between N-actetylmuramoyl and N-acetylglucosaminyl residues with the concomitant ...
Scheurwater, Edie +2 more
openaire +4 more sources
A SpoIID Homolog Cleaves Glycan Strands at the Chlamydial Division Septum
Chlamydiales species are obligate intracellular bacteria lacking a classical peptidoglycan sacculus but relying on peptidoglycan synthesis for cytokinesis.
Nicolas Jacquier +5 more
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Peptidoglycan lytic activity of thePseudomonas aeruginosaphage ÏKZ gp144 lytic transglycosylase [PDF]
The gp144 endolysin gene from the Pseudomonas aeruginosa phage phiKZ was cloned and studies of gp144 expression into Escherichia coli showed host cell lysis. The gp144 protein was purified directly from the culture supernatant and from the bacterial cell pellet and showed in vitro antibacterial lytic activity against P. aeruginosa bacteria and degraded
Catherine, Paradis-Bleau +7 more
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Staphylococcal bacteriophages of the Kayvirus genus are candidates for therapeutic applications. One of their proteins, Tgl, is slightly similar to two staphylococcal virulence factors, secreted autolysins of lytic transglycosylase motifs IsaA and SceD ...
Aleksandra Głowacka-Rutkowska +5 more
doaj +1 more source
Crystallographic Studies of the Interactions of Escherichia coli Lytic Transglycosylase Slt35 with Peptidoglycan [PDF]
Lytic transglycosylases catalyze the cleavage of the β-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydro bond in the MurNAc residue.
Kor H. Kalk +8 more
core +1 more source

