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Plant Physiology 96:310-313 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Acetolactate Synthase Inhibiting Herbicides Bind to the Regulatory Site

Mani V. Subramanian, Vivian Loney-Gallant, Jennifer M. Dias and Linda C. Mireles

DowElanco, Walnut Creek, California 94598

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.




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Copyright © 1991 by the American Society of Plant Biologists