Inhibition of Membrane-bound Lytic Transglycosylase B by NAG-thiazoline
The lytic transglycosylases cleave the bacterial cell wall heteropolymer peptidoglycan with the same specificity as the muramidases (lysozymes), between the N-acetylmuramic acid and N-acetylglucosamine residues, with the concomitant formation of a 1,6-anhydromuramoyl residue. The putative catalytic residue in the family 3 lytic transglycosylase from Pseudomonas aeruginosa, Glu162 as identified by sequence alignment to the homologous enzyme from Escherichia coli, was replaced with both Ala and Asp by site-directed mutagenesis.
Recommended CitationReid, Christopher W.; Blackburn, N. T.; Legaree, Blaine A.; Auzanneau, F. I.; and Clarke, Anthony J., "Inhibition of Membrane-bound Lytic Transglycosylase B by NAG-thiazoline" (2004). Science and Technology Faculty Journal Articles. Paper 42.
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