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PLANT PHYSIOLOGY , Vol 106, Issue 4 1257-1260, Copyright © 1994 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Inhibition of Threonine Dehydratase Is Herbicidal

I. T. Szamosi, D. L. Shaner and B. K. Singh
American Cyanamid Company, P.O. Box 400, Princeton, New Jersey 08543-0400

Threonine dehydratase, the first enzyme in isoleucine biosynthesis, catalyzes deamination and dehydration of threonine to produce 2-ketobutyrate and ammonia. An antimetabolite, 2-(1-cyclohexen-3(R)-yl)-S-glycine (CHG), inhibits the plant enzyme. CHG inhibits the growth of Black Mexican Sweet corn (Zea mays) cells and of Arabidopsis thaliana plants. The herbicidal effects of CHG can be reversed by 2-ketobutyrate, other intermediates of isoleucine biosynthesis, and by isoleucine itself. These results suggest that the herbicidal effects observed with CHG are a consequence of inhibition of threonine dehydratase. The enzyme could be a potential target site for an herbicide screening program.




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Copyright © 1994 by the American Society of Plant Biologists