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Molecular Basis of Sulfonylurea Herbicide Inhibition of Acetohydroxyacid Synthase
Open accessAbstract
Acetohydroxyacid synthase (AHAS) (acetolactate synthase, EC ) catalyzes the first step in branched-chain amino acid biosynthesis and is the target for sulfonylurea and imidazolinone herbicides. These compounds are potent and selective inhibitors, but their binding site on AHAS has not been elucidated. Here we report the 2.8 A resolution crystal structure of yeast AHAS in complex with a sulfonylurea herbicide, chlorimuron ethyl. The inhibitor, which has a K(i) of 3.3 nm, blocks access to the active site and contacts multiple residues where mutation results in herbicide resistance. The structure provides a starting point for the rational design of further herbicidal compounds.
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Cited by
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The unique role of halogen substituents in the design of modern agrochemicals
Jeschke, P. (2010) · Pest Management Science · doi:10.1002/ps.1829 · Cited by 593
Resistance to AHAS inhibitor herbicides: current understanding
Yu, Q., & Powles, S. B. (2014) · Pest Management Science · doi:10.1002/ps.3710 · Cited by 472
Metadata
- Authors
- Pang, S. S., Guddat, L. W., & Duggleby, R. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 278
- Issue
- 9
- Pages
- 7639-7644
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2136665220
- Cited by
- 172
- References
- 0
- FWCI
- 8.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Pang, S. S., Guddat, L. W., & Duggleby, R. G. (2003). Molecular Basis of Sulfonylurea Herbicide Inhibition of Acetohydroxyacid Synthase. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m211648200
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