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The Lysozyme Inhibitor Thionine Acetate Is Also an Inhibitor of the Soluble Lytic Transglycosylase Slt35 from Escherichia coli.

Authors :
Mezoughi, Aysha B.
Costanzo, Chiara M.
Parker, Gregor M.
Behiry, Enas M.
Scott, Alan
Wood, Andrew C.
Adams, Sarah E.
Sessions, Richard B.
Loveridge, E. Joel
Source :
Molecules; Jul2021, Vol. 26 Issue 14, p4189-4189, 1p
Publication Year :
2021

Abstract

Lytic transglycosylases such as Slt35 from E. coli are enzymes involved in bacterial cell wall remodelling and recycling, which represent potential targets for novel antibacterial agents. Here, we investigated a series of known glycosidase inhibitors for their ability to inhibit Slt35. While glycosidase inhibitors such as 1-deoxynojirimycin, castanospermine, thiamet G and miglitol had no effect, the phenothiazinium dye thionine acetate was found to be a weak inhibitor. IC<subscript>50</subscript> values and binding constants for thionine acetate were similar for Slt35 and the hen egg white lysozyme. Molecular docking simulations suggest that thionine binds to the active site of both Slt35 and lysozyme, although it does not make direct interactions with the side-chain of the catalytic Asp and Glu residues as might be expected based on other inhibitors. Thionine acetate also increased the potency of the beta-lactam antibiotic ampicillin against a laboratory strain of E. coli. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
14203049
Volume :
26
Issue :
14
Database :
Complementary Index
Journal :
Molecules
Publication Type :
Academic Journal
Accession number :
151612982
Full Text :
https://doi.org/10.3390/molecules26144189