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

Aysha B. Mezoughi, Chiara Costanzo, Gregor M. Parker, Enas M. Behiry, Alan Scott, Andrew C. Wood, Sarah E. Adams, Richard B. Sessions, Joel Loveridge Orcid Logo

Molecules, Volume: 26, Issue: 14, Start page: 4189

Swansea University Authors: Chiara Costanzo, Joel Loveridge Orcid Logo

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DOI (Published version): 10.3390/molecules26144189

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 glycosi...

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Published in: Molecules
ISSN: 1420-3049
Published: MDPI AG 2021
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URI: https://cronfa.swan.ac.uk/Record/cronfa57288
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 Description: Data are contained within the article or Supplementary Materials.
Keywords: lytic transglycosylase; thionine acetate; enzyme inhibition; antibacterial
College: Faculty of Science and Engineering
Funders: This research was funded by the UK Biotechnology and Biological Sciences Research Council (BBSRC), grant number BB/L01758X/1; the Life Sciences Research Network Wales, grant number NRNRG4Mar039; the Libyan Embassy (London), PhD studentship 10007 to A.B.A.M.; the Royal Society of Chemistry, Undergraduate Research Bursary to G.M.P.; Cardiff University and Swansea University. The APC was funded by Swansea University.
Issue: 14
Start Page: 4189

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