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
Comparative Genomics of 9 Novel Paenibacillus Larvae Bacteriophages [PDF]
American Foulbrood Disease, caused by the bacterium Paenibacillus larvae, is one of the most destructive diseases of the honeybee, Apis mellifera. Our group recently published the sequences of 9 new phages with the ability to infect and lyse P.
Amy, Penny S. +4 more
core +2 more sources
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
doaj +1 more source
The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes [PDF]
Resuscitation-promoting factor (RPF) proteins reactivate stationary-phase cultures of (G+C)-rich Gram-positive bacteria including the causative agent of tuberculosis, Mycobacterium tuberculosis.
AT Brunger +27 more
core +2 more sources
Molecular characterisation, evolution and expression analysis of g-type lysozymes in Ciona intestinalis [PDF]
Lysozyme is an important defense molecule of the innate immune system. Known for its bactericidal properties, lysozyme catalyzes the hydrolysis of b-(1,4)-glycosidic bonds between the N-acetyl glucosamine and N-acetyl muramic acid in the peptidoglycan ...
Cammarata, M., Di Falco, F., Vizzini, A.
core +1 more source
Characterization ofHelicobacter pyloriLytic Transglycosylases Slt and MltD [PDF]
ABSTRACTPeptidoglycan (PG) is a cell wall heteropolymer that is essential for cell integrity. PG hydrolases participate in correct assembly of the PG layer and have been shown to be required for cell division, cell daughter separation, and maintenance of bacterial morphology. In silico analysis of theHelicobacter pylorigenome resulted in identification
Catherine Chaput +2 more
openalex +4 more sources
Assembly of the bacterial flagellar rod, hook, and filament requires penetration through the peptidoglycan (PG) sacculus and outer membrane. In most β- and γ-proteobacteria, the protein FlgJ has two functional domains that enable PG hydrolyzing activity ...
Hui Xu +6 more
doaj +1 more source

