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植物乙酰羟酸合酶的抑制结构与机制

Structure and mechanism of inhibition of plant acetohydroxyacid synthase.

作者信息

Duggleby Ronald G, McCourt Jennifer A, Guddat Luke W

机构信息

RDBiotech, 22 Parklands Boulevard, Little Mountain, Queensland 4551, Australia.

出版信息

Plant Physiol Biochem. 2008 Mar;46(3):309-24. doi: 10.1016/j.plaphy.2007.12.004. Epub 2008 Jan 14.

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.

摘要

植物和微生物通过一条共同途径合成缬氨酸、亮氨酸和异亮氨酸,该途径的第一步反应由乙酰羟酸合酶(AHAS,EC 2.2.1.6)催化。这种酶至关重要,因为它是几种除草剂的作用靶点,包括广受欢迎的磺酰脲类和咪唑啉酮类的所有成员。然而,由于干扰AHAS抑制作用的突变导致抗性杂草的出现,如今已成为一个全球性问题。在此,我们基于拟南芥AHAS的三维结构,总结了关于这些除草剂抑制该酶方式的最新观点。该结构还揭示了理解各种突变如何导致除草剂抗性的重要线索。

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