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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail
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Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail

机译：除草剂草甘膦与其靶酶5-烯丙基丙酮酸shi草酸酯3-磷酸合酶的相互作用详细

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摘要

Biosynthesis of aromatic amino acids in plants, many bacteria, and microbes relies on the enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, a prime target for drugs and herbicides. We have identified the interaction of EPSP synthase with one of its two substrates (shikimate 3-phosphate) and with the widely used herbicide gIyphosate by x-ray crystallography. The two-domain enzyme closes on ligand binding. thereby forming the active site in the interdomain cleft. Glyphosate appears to occupy the binding site of the second substrate of EPSP synthase (phosphoenol pyruvate), mimicking an interme- diate state of the ternary enzyme. substrates complex. The elucidation of the active site of EPSP synthase and especially of the binding pattern of glyphosate provides a valuable roadmap for engineering new herbicides and herbicide-resistant crops, as well as new antibiotic and antiparasitic drugs.
机译：植物，许多细菌和微生物中芳香族氨基酸的生物合成依赖于3-enolpyruvylshikimate 3-phosphate（EPSP）合酶，这是药物和除草剂的主要靶标。我们已经通过X射线晶体学鉴定了EPSP合酶与其两种底物之一（Shikimate 3-phosphate）以及广泛使用的除草剂草甘膦的相互作用。两结构域酶在配体结合时关闭。从而在域间裂隙中形成活性位点。草甘膦似乎占据了EPSP合酶第二种底物（磷酸烯醇丙酮酸）的结合位点，模仿了三元酶的中间状态。底物复杂。阐明EPSP合酶的活性位点，尤其是草甘膦的结合模式，为设计新的除草剂和抗除草剂作物以及新型抗生素和抗寄生虫药物提供了宝贵的路线图。

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