Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis in plants.

doi:10.1104/PP.75.3.827

Paper

Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis in plants.

Published Jul 1, 1984 · T. Ray

Plant physiology

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604

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28

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Abstract

The sulfonylurea herbicide chlorsulfuron blocks the biosynthesis of the amino acids valine and isoleucine in plants. Addition of these two amino acids to excised pea root (Pisum sativum L. var Alaska) cultures incubated in the presence of chlorsulfuron completely alleviates herbicide-induced growth inhibition. The site of action of chlorsulfuron is the enzyme acetolactate synthase which catalyzes the first step in the biosynthesis of valine and isoleucine. This enzyme is extremely sensitive to inhibition by chlorsulfuron having I(50) values ranging from 18 to 36 nanomolar. In addition, acetolactate synthase from a wide variety of tolerant and sensitive plants species is highly sensitive to inhibition by chlorsulfuron.

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Study Snapshot

Chlorsulfuron herbicide inhibits plant growth by blocking the biosynthesis of amino acids valine and isoleucine, with acetolactate synthase being highly sensitive to inhibition.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis in plants.

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