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Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase
Wang, JG; Lee, PKM; 董宇辉Dong, YH; Pang, SS; Duggleby, RG; Li, ZM; Guddat, LW
2009
发表期刊FEBS JOURNAL
卷号276期号:5页码:1282-1290
通讯作者[Wang, Jian-Guo ; Li, Zheng-Ming] Nankai Univ, Natl Pesticide Engn Res Ctr, State Key Lab Elementoorgan Chem, Tianjin 300071, Peoples R China ; [Lee, Patrick K-M. ; Pang, Siew Siew ; Duggleby, Ronald G. ; Guddat, Luke W.] Univ Queensland, Sch Mol & Microbial Sci, Brisbane, Qld, Australia ; [Dong, Yu-Hui] Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100039, Peoples R China
文章类型Article
摘要Acetohydroxyacid synthase (AHAS; EC 2.2.1.6) is the first enzyme in the biosynthetic pathway of the branched-chain amino acids. It catalyzes the conversion of two molecules of pyruvate into 2-acetolactate or one molecule of pyruvate and one molecule of 2-ketobutyrate into 2-aceto-2-hydroxybutyrate. AHAS requires the cofactors thiamine diphosphate (ThDP), Mg(2+) and FAD for activity. The herbicides that target this enzyme are effective in protecting a broad range of crops from weed species. However, resistance in the field is now a serious problem worldwide. To address this, two new sulfonylureas, monosulfuron and monosulfuron ester, have been developed as commercial herbicides in China. These molecules differ from the traditional sulfonylureas in that the heterocyclic ring attached to the nitrogen atom of the sulfonylurea bridge is monosubstituted rather than disubstituted. The structures of these compounds in complex with the catalytic subunit of Arabidopsis thaliana AHAS have been determined to 3.0 and 2.8 angstrom, respectively. In both complexes, these molecules are bound in the tunnel leading to the active site, such that the sole substituent of the heterocyclic ring is buried deepest and oriented towards the ThDP. Unlike the structures of Arabidopsis thaliana AHAS in complex with the classic disubstituted sulfonylureas, where ThDP is broken, this cofactor is intact and present most likely as the hydroxylethyl intermediate.
关键词acetohydroxyacid synthase branched-chain amino acids crystal structure herbicide sulfonylurea
学科领域Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology ; Biochemistry & Molecular Biology
DOI10.1111/j.1742-4658.2009.06863.x
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语种英语
研究领域[WOS]Biochemistry & Molecular Biology ; Biochemistry & Molecular Biology
WOS类目Biochemistry & Molecular Biology
WOS记录号WOS:000263451600012
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被引频次:34[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/239251
专题多学科研究中心
作者单位中国科学院高能物理研究所
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Wang, JG,Lee, PKM,董宇辉Dong, YH,et al. Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase[J]. FEBS JOURNAL,2009,276(5):1282-1290.
APA Wang, JG.,Lee, PKM.,董宇辉Dong, YH.,Pang, SS.,Duggleby, RG.,...&Guddat, LW.(2009).Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase.FEBS JOURNAL,276(5),1282-1290.
MLA Wang, JG,et al."Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase".FEBS JOURNAL 276.5(2009):1282-1290.
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