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Updated: Jul 7, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Structure and mechanism of inhibition of plant acetohydroxyacid synthase
Ronald G Duggleby1, Jennifer A McCourt, Luke W Guddat
1RDBiotech, 22 Parklands Boulevard, Little Mountain, Queensland 4551, Australia. ron_duggleby@fastmail.com.au
Abstract:
Plants and microorganisms synthesize valine, leucine and isoleucine via a common pathway in which the first reaction is catalysed by acetohydroxyacid synthase (AHAS, EC 2.2.1.6). This enzyme is of substantial importance because it is the target of several herbicides, including all members of the popular sulfonylurea and imidazolinone families. However, the emergence of resistant weeds due to mutations that interfere with the inhibition of AHAS is now a worldwide problem. Here we summarize recent ideas on the way in which these herbicides inhibit the enzyme, based on the 3D structure of Arabidopsis thaliana AHAS. This structure also reveals important clues for understanding how various mutations can lead to herbicide resistance.
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