The activity of the enzyme, acetolactate synthase, extracted from cultured, wild-type cells of Datura innoxia P. Mill. was inhibited by valine and leucine (5-20 mM), added either separately or together, and by chlorsulfuron (10-8and 10-5M). Isoleucine (5-20 mM) was a weaker inhibitor than valine and leucine. Acetolactate synthase isolated from four chlorsulfuron-resistant, D. innoxia cell variants was also tested for feedback sensitivity to the three amino acids. Results showed that the acetolactate synthase from chlorsulfuron-resistant variants had less feedback sensitivity to valine, leucine and isoleucine added to assay mixtures either separately or in combination, compared to the enzyme from wild-type cells. © 1990.
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