Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors

被引：191

作者：

Pang, SS ^{[1
]}

Duggleby, RG ^{[1
]}

Guddat, LW ^{[1
]}

机构：

[1] Univ Queensland, Sch Mol & Microbial Sci, Dept Biochem & Mol Biol, Ctr Prot Struture Funct & Engn, Brisbane, Qld 4072, Australia

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 317卷 / 02期

基金：

澳大利亚研究理事会;

关键词：

acetohydroxyacid synthase; acetolactate synthase; FAD; thiamin diphosphate; herbicide inhibition;

D O I：

10.1006/jmbi.2001.5419

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Acetohydroxyacid synthase (AHAS; EC 4.1.3.18) catalyzes the first step in branched-chain amino acid biosynthesis. The enzyme requires thiamin diphosphate and FAD for activity, but the latter is unexpected, because the reaction involves no oxidation or reduction. Due to its presence in plants, AHAS is a target for sulfonylurea and imidazolinone herbicides. Here, the crystal structure to 2.6 A resolution of the catalytic subunit of yeast AHAS is reported. The active site is located at the dimer interface and is near the proposed herbicide-binding site. The conformation of FAD and its position in the active site are defined. The structure of AHAS provides a starting point for the rational design of new herbicides. (C) 2002 Elsevier Science Ltd.

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页码：249 / 262

页数：14

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