Threonine dehydratase, the first enzyme in isoleucine biosynthesis, ca
talyzes deamination and dehydration of threonine to produce 2-ketobuty
rate and ammonia. An antimetabolite, 2-(1-cyclohexen-3(R)-yl)-S-glycin
e (CHG), inhibits the plant enzyme. CHG inhibits the growth of Black M
exican Sweet corn (Zea mays) cells and of Arabidopsis thaliana plants.
The herbicidal effects of CHG can be reversed by 2-ketobutyrate, othe
r intermediates of isoleucine biosynthesis, and by isoleucine itself.
These results suggest that the herbicidal effects observed with CHG ar
e a consequence of inhibition of threonine dehydratase. The enzyme cou
ld be a potential target site for an herbicide screening program.