Molecular basis of triclosan activity

Colin W. Levy, Anna Roujeinikova, Svetlana Sedelnikova, Patrick J. Baker, Antoine R. Stuitje, Antoni R. Slabas (), David W. Rice and John B. Rafferty
Additional contact information
Colin W. Levy: Krebs Institute for Biomolecular Research, University of Sheffield
Anna Roujeinikova: Krebs Institute for Biomolecular Research, University of Sheffield
Svetlana Sedelnikova: Krebs Institute for Biomolecular Research, University of Sheffield
Patrick J. Baker: Krebs Institute for Biomolecular Research, University of Sheffield
Antoine R. Stuitje: Institute of Molecular Biological Studies (IMBW), Vrije Universiteit
Antoni R. Slabas: University of Durham
David W. Rice: Krebs Institute for Biomolecular Research, University of Sheffield
John B. Rafferty: Krebs Institute for Biomolecular Research, University of Sheffield

Nature, 1999, vol. 398, issue 6726, 383-384

Abstract: Abstract Triclosan (5-chloro-2-(2,4-dichlorophenoxy) phenol) has been used for more than 30 years as a general antibacterial and antifungal agent, and is found in formulations as diverse as toothpastes, cosmetics, antiseptic soaps, carpets, plastic kitchenware and toys. It has recently been suggested that triclosan blocks lipid biosynthesis by specifically inhibiting the enzyme enoyl-acyl carrier protein reductase (ENR)1. We have carried out a structural analysis and inhibition experiments on a complex of ENR from the bacterium Escherichia coli with triclosan and NAD+. We find that triclosan acts as a site-directed, very potent inhibitor of the enzyme by mimicking its natural substrate.

Date: 1999
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DOI: 10.1038/18803

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