DigitalCommons@Bryant University

Title

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

Authors

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

Document Type

Article

Comments

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

Bryant University users may access this article here.

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.

Recommended Citation

Reid, 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.
http://digitalcommons.bryant.edu/sci_jou/42