Title

Substrate Binding Affinity of Pseudomonas Aeruginosa Membrane-Bound Lytic Transglycosylase B by Hydrogen−Deuterium Exchange MALDI MS

Document Type

Article

Comments

Published by ACS Publications in Biochemistry, Volume 43, pages 11275-11282.

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Publication Source

Biochemistry

Abstract

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.

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