Inhibition of Membrane-bound Lytic Transglycosylase B by NAG-thiazoline

Document Type



Published by the Federation of European Biochemical Societies in FEBS Letters, Volume 574, Issues 1-3, pages 73-79.

Users may access this article here.

Publication Source

FEBS Letters


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.