Hostname: page-component-6898cfcb55-th4rj Total loading time: 0 Render date: 2026-11-11T12:25:09.332Z Has data issue: false hasContentIssue false

Herbicides that Inhibit Acetohydroxyacid Synthase

Published online by Cambridge University Press:  12 June 2017

Mark A. Stidham*
Affiliation:
Agric. Res. Div., American Cyanamid Co., Princeton, NJ 08543-0400, U.S.A.

Abstract

Acetohydroxyacid synthase was discovered as the site of action of imidazolinone and sulfonylurea herbicides over 6 yr ago. In recent years, advances have been made in the understanding of this enzyme as a herbicide target site. Derivatives of both imidazolinones and sulfonylureas have yielded new herbicide chemistry. AH of the herbicides display unusual “slow-binding” behavior with the enzyme, and this behavior may help explain efficacy of the herbicides. Resistance to these herbicides has been developed through a number of different procedures, and the mechanism of resistance is through changes in sensitivity of the enzyme to the herbicides. The changes are either selective to only one class of chemistry, or broad to a number of classes of chemistry. These data support the idea that binding sites for the herbicides on the enzyme are only partially overlapping. Progress in purification of AHAS from corn includes discovery of the existence of the enzyme in monomer and oligomer aggregation states. The interaction of the enzyme with the herbicides is affected by enzyme aggregation state.

Information

Type
Special Topics
Copyright
Copyright © 1991 by the Weed Science Society of America 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Article purchase

Temporarily unavailable