Acetolactate synthase inhibiting herbicides bind to the regulatory site.
نویسندگان
چکیده
Acetolactate synthase from spontaneous mutants of tobacco (Nicotiana tabacum; KS-43 and SK-53) and cotton (Gossypium hirsutum; PS-3, PSH-91, and DO-2) selected in tissue culture for resistance to a triazolopyrimidine sulfonanilide showed varying degrees of insensitivity to feedback inhibitor(s) valine and/or leucine. A similar feature was evident in the enzyme isolated from chlorsulfuron-resistant weed biotypes, Kochia scoparia and Stellaria media. Dual inhibition analyses of triazolopyrimidine sulfonanilide, thifensulfuron, and imazethapyr versus feedback inhibitor leucine revealed that the three herbicides were competitive with the amino acid for binding to acetolactate synthase from wild-type cotton cultures. Acetolactate synthase inhibiting herbicides may bind to the regulatory site on the enzyme.
منابع مشابه
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Malathion in mixture with acetolactate synthase (ALS)-inhibiting herbicides synergizes the control of weed species that have evolved metabolism-based resistance to ALS-inhibiting herbicides. However, the effect of malathion-based herbicide programs on conventional and imidazolinone-resistant (Clearfield) rice systems still need to be evaluated. Studies were conducted to determine the tolerance ...
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ورودعنوان ژورنال:
- Plant physiology
دوره 96 1 شماره
صفحات -
تاریخ انتشار 1991