EloR interacts with the lytic transglycosylase MltG at midcell in Streptococcus pneumoniae R6. [PDF]
AbstractThe ellipsoid shape ofStreptococcus pneumoniaeis determined by the synchronized actions of the elongasome and the divisome, which have the task of creating a protective layer of peptidoglycan (PG) enveloping the cell membrane. The elongasome is necessary for expanding PG in the longitudinal direction whereas the divisome synthesizes the PG that
Winther AR +4 more
europepmc +5 more sources
Structure of the Bacteriophage φKZ Lytic Transglycosylase gp144 [PDF]
Lytic transglycosylases are enzymes that act on the peptidoglycan of bacterial cell walls. They cleave the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues with the concomitant formation of a 1,6-anhydromuramoyl product. The x-ray structure of the lytic transglycosylase gp144 from the Pseudomonas bacteriophage phi KZ has ...
Andrei, Fokine +4 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
doaj +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
Characterization of three different lytic transglycosylases inEscherichia coli [PDF]
Two lytic transglycosylases, releasing 1,6-anhydromuropeptides from murein sacculi are present in a mutant deleted for the soluble lytic transglycosylase 70 (Slt70). Thus, there are three different lytic transglycosylases in Escherichia coli. One of the remaining enzymes is soluble and one is a membrane protein that can be solubilized by 2% Triton X ...
Romeis T, Vollmer W, Höltje J-V
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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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Crystallization of the soluble lytic transglycosylase from Escherichia coli K12 [PDF]
Lytic transglycosylases degrade the murein polymer of the bacterial cell wall to 1,6-anhydromuropeptides. These enzymes are of significant medical interest, not only because they are ideal targets for the development of new classes of antibiotics, but also because the low molecular weight products of their catalytic action can cause diverse biological ...
Rozeboom, Henriette J. +3 more
openaire +3 more sources
The Effect of NAG–thiazoline on Morphology and Surface Hydrophobicity of Escherichia Coli [PDF]
The β-hexosaminidase inhibitor and structural analog of the putative oxazolium reaction intermediate of lytic transglycosylases, N-acetylglucosamine thiazoline (NAG–thiazoline), was synthesized in 46% overall yield and tested as an inhibitor of ...
Blackburn, Neil T. +2 more
core +2 more sources
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
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

