Substrate Binding Affinity of Pseudomonas Aeruginosa Membrane-Bound Lytic Transglycosylase B by Hydrogen−Deuterium Exchange MALDI MS
Lytic transglycosylases cleave the β-(1→4)-glycosidic bond in the bacterial cell wall heteropolymer, peptidoglycan, between the N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues with the concomitant formation of a 1,6-anhydromuramoyl residue. With 72% amino acid sequence identity between the enzymes, the theoretical structure of the membrane-bound lytic transglycosylase B (MltB) from Psuedomonas aeruginosa was modeled on the known crystal structure of Escherichia coli Slt35, the soluble derivative of its MltB.
Recommended CitationReid, Christopher W.; Brewer, Dyanne; and Clarke, Anthony J., "Substrate Binding Affinity of Pseudomonas Aeruginosa Membrane-Bound Lytic Transglycosylase B by Hydrogen−Deuterium Exchange MALDI MS" (2004). Science and Technology Faculty Journal Articles. Paper 37.
This document is currently not available here.