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The lysozyme inhibitor thionine acetate is also an inhibitor of the soluble lytic transglycosylase Slt35 from escherichia coli

Mezoughi, Aysha B., Costanzo, Chiara M., Parker, Gregor M., Behiry, Enas M., Scott, Alan, Wood, Andrew C., Adams, Sarah E., Sessions, Richard B. and Loveridge, E. Joel 2021. The lysozyme inhibitor thionine acetate is also an inhibitor of the soluble lytic transglycosylase Slt35 from escherichia coli. Molecules 26 (14) , 4189. 10.3390/molecules26144189

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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. IC50 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.

Item Type: Article
Date Type: Published Online
Status: Published
Schools: Chemistry
Additional Information: This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/ licenses/by/4.0/).
Publisher: MDPI
ISSN: 1420-3049
Funders: BBSRC
Date of First Compliant Deposit: 26 July 2021
Date of Acceptance: 6 July 2021
Last Modified: 29 Jul 2021 09:15
URI: http://orca.cardiff.ac.uk/id/eprint/142882

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