Title

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

Authors

Christopher W. Reid, Bryant University
Neil T. Blackburn
Blaine A. Legaree
F. I. Auzanneau
Anthony J. ClarkeFollow

Document Type

Article

Comments

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

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Keywords

Lytic transglycosylase;Peptidoglycan;Inhibition;Catalytic residue;Mechanism;Pseudomonas aeruginosa

Publisher

Federation of European Biochemical Societies

Publication Source

FEBS Letters

Abstract

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.