ArticleThe Biochemical journal1998
Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase: characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 97 citations in OpenAlex.
- Isoform-specific function underlies differential herbicide resistance of the W574L mutation in peanut AhALS isozymes.Pest management science · 2026Article
- Triazolopyrimidine herbicides are potent inhibitors of Aspergillus fumigatus acetohydroxyacid synthase and potential antifungal drug leads.Scientific reports · 2021Article
- Engineering Herbicide-Tolerance Rice Expressing an Acetohydroxyacid Synthase with a Single Amino Acid Deletion.International journal of molecular sciences · 2020Article
- Commercial AHAS-inhibiting herbicides are promising drug leads for the treatment of human fungal pathogenic infections.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Comprehensive understanding of acetohydroxyacid synthase inhibition by different herbicide families.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Transformation of apple (Malus × domestica) using mutants of apple acetolactate synthase as a selectable marker and analysis of the T-DNA integration sites.Plant cell reports · 2013Article
- Response to imazapyr and dominance relationships of two imidazolinone-tolerant alleles at the Ahasl1 locus of sunflower.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2012Article
- Expression, characterization, and site-directed mutation of a multiple herbicide-resistant acetohydroxyacid synthase (rAHAS) from Pseudomonas sp. Lm10.Current microbiology · 2011Article
- AHAS herbicide resistance endowing mutations: effect on AHAS functionality and plant growth.Journal of experimental botany · 2010Article
- Multiple allelic forms of acetohydroxyacid synthase are responsible for herbicide resistance in Setaria viridis.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2009Article
- Aspartate-Derived Amino Acid Biosynthesis in Arabidopsis thaliana.The arabidopsis book · 2009Article
- Selectable tolerance to herbicides by mutated acetolactate synthase genes integrated into the chloroplast genome of tobacco.Plant physiology · 2008Article
- Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Structure-activity relationships for a new family of sulfonylurea herbicides.Journal of computer-aided molecular design · 2005Article
- Effects of deletions at the C-terminus of tobacco acetohydroxyacid synthase on the enzyme activity and cofactor binding.The Biochemical journal · 2004Article
- A novel selection system for potato transformation using a mutated AHAS gene.Plant cell reports · 2003Article
- Ethylmethanesulfonate saturation mutagenesis in Arabidopsis to determine frequency of herbicide resistance.Plant physiology · 2003Article
- Mutagenesis studies on the sensitivity of Escherichia coli acetohydroxyacid synthase II to herbicides and valine.The Biochemical journal · 2000Article
- Mutagenesis of Escherichia coli acetohydroxyacid synthase isoenzyme II and characterization of three herbicide-insensitive forms.The Biochemical journal · 1998Article
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2 authors at 1 institution in 1 country.
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Abstract
Acetohydroxyacid synthase (AHAS) catalyses the first step in the synthesis of the branched-chain amino acids and is the target of several classes of herbicides. Four mutants (A122V, W574S, W574L and S653N) of the AHAS gene from Arabidopsis thaliana were constructed, expressed in Escherichia coli, and the enzymes were purified. Each mutant form and wild-type was characterized with respect to its catalytic properties and sensitivity to nine herbicides. Each enzyme had a pH optimum near 7.5. The specific activity varied from 13% (A122V) to 131% (W574L) of the wild-type and the Km for pyruvate of the mutants was similar to the wild-type, except for W574L where it was five-fold higher. The activation by cofactors (FAD, Mg2+ and thiamine diphosphate) was examined. A122V showed reduced affinity for all three cofactors, whereas S653N bound FAD more strongly than wild-type AHAS. Six sulphonylurea herbicides inhibited A122V to a similar degree as the wild-type but S653N showed a somewhat greater reduction in sensitivity to these compounds. In contrast, the W574 mutants were insensitive to these sulphonylureas, with increases in the Kiapp (apparent inhibition constant) of several hundred fold. All four mutants were resistant to three imidazolinone herbicides with decreases in sensitivity ranging from 100-fold to more than 1000-fold.
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