Structure and mechanism of inhibition of plant acetohydroxyacid synthase

被引：287

作者：

Duggleby, Ronald G. ^{[1
]}

McCourt, Jennifer A. ^{[1
]}

Guddat, Luke W. ^{[2
]}

机构：

[1] RDBiotech, Little Mt, Qld 4551, Australia

[2] Univ Queensland, Sch Mol & Microbial Sci, Brisbane, Qld 4072, Australia

来源：

PLANT PHYSIOLOGY AND BIOCHEMISTRY | 2008年 / 46卷 / 03期

关键词：

acetohydroxyacid synthase; branched-chain amino acids; herbicide; inhibitor; protein structure; herbicide resistance;

D O I：

10.1016/j.plaphy.2007.12.004

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

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. (c) 2007 Elsevier Masson SAS. All rights reserved.

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收藏

页码：309 / 324

页数：16

相关论文

共 70 条

[1] OXYGENASE SIDE REACTIONS OF ACETOLACTATE SYNTHASE AND OTHER CARBANION-FORMING ENZYMES [J].

ABELL, LM ;

SCHLOSS, JV .

BIOCHEMISTRY, 1991, 30 (32) :7883-7887

[2] A NATURALLY-OCCURRING POINT MUTATION CONFERS BROAD RANGE TOLERANCE TO HERBICIDES THAT TARGET ACETOLACTATE SYNTHASE [J].

BERNASCONI, P ;

WOODWORTH, AR ;

ROSEN, BA ;

SUBRAMANIAN, MV ;

SIEHL, DL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (29) :17381-17385

[3] Structural changes in a cryo-cooled protein crystal owing to radiation damage [J].

Burmeister, WP .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2000, 56 :328-341

[4] ACETOLACTATE SYNTHASE IS THE SITE OF ACTION OF 2 SULFONYLUREA HERBICIDES IN HIGHER-PLANTS [J].

CHALEFF, RS ;

MAUVAIS, CJ .

SCIENCE, 1984, 224 (4656) :1443-1445

[5] Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase:: characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants [J].

Chang, AK ;

Duggleby, RG .

BIOCHEMICAL JOURNAL, 1998, 333 :765-777

[6] Expression, purification and characterization of Arabidopsis thaliana acetohydroxyacid synthase [J].

Chang, AK ;

Duggleby, RG .

BIOCHEMICAL JOURNAL, 1997, 327 :161-169

[7] Mechanisms of acetohydroxyacid synthases [J].

Chipman, DM ;

Duggleby, RG ;

Tittmann, K .

CURRENT OPINION IN CHEMICAL BIOLOGY, 2005, 9 (05) :475-481

[8] Amino acid residues conferring herbicide tolerance in tobacco acetolactate synthase [J].

Chong, CK ;

Choi, JD .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 279 (02) :462-467

[9] High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis -: Implications for substrate activation in pyruvate decarboxylases [J].

Dobritzsch, D ;

König, S ;

Schneider, G ;

Lu, GG .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (32) :20196-20204

[10] Systematic characterization of mutations in yeast acetohydroxyacid synthase - Interpretation of herbicide-resistance data [J].

Duggleby, RG ;

Pang, SS ;

Yu, HQ ;

Guddat, LW .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2003, 270 (13) :2895-2904

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