Title of article
Structure and mechanism of inhibition of plant acetohydroxyacid synthase
Author/Authors
Duggleby، نويسنده , , Ronald G. and McCourt، نويسنده , , Jennifer A. and Guddat، نويسنده , , Luke W.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2008
Pages
16
From page
309
To page
324
Abstract
Plants and microorganisms synthesize valine, leucine and isoleucine via a common pathway in which the first reaction is catalysed by acetohydroxyacid synthase (AHAS, EC 2.2.1.6). This enzyme is of substantial importance because it is the target of several herbicides, including all members of the popular sulfonylurea and imidazolinone families. However, the emergence of resistant weeds due to mutations that interfere with the inhibition of AHAS is now a worldwide problem. Here we summarize recent ideas on the way in which these herbicides inhibit the enzyme, based on the 3D structure of Arabidopsis thaliana AHAS. This structure also reveals important clues for understanding how various mutations can lead to herbicide resistance.
Keywords
protein structure , Herbicide resistance , acetohydroxyacid synthase , branched-chain amino acids , Herbicide , Inhibitor
Journal title
Plant Physiology and Biochemistry
Serial Year
2008
Journal title
Plant Physiology and Biochemistry
Record number
2121822
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