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首页> 外文期刊>Biochemistry >Shikimate-3-phosphate binds to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase
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Shikimate-3-phosphate binds to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase

机译：磷酸Shikimate-3-磷酸结合到5-enolpyruvylshikimate-3-磷酸合酶的N末端结构域

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摘要

5-Eno1pyruvylshikimate-3-PhosPhate (EPSP) synthase catalyzes the transfer of the enolpyruvyl moiety from phosphoenolpyruvate (PEP) to shikimate-3-phosphate (S3P). Mutagenesis and X-ray crystallography data suggest that the active site of the enzyme is in the cleft between its two globular domains; however, they have not defined which residues are responsible for substrate binding and catalysis. Here we attempt to establish the binding of the substrate S3P to the isolated N-terminal domain of EPSP synthase using a combination of NMR spectroscopy and isothermal titration calorimetry. Our expenmental results indicate that there is a saturable and stable conformational change in the isolated N-terminal domain upon S3P binding and that the chemical environment of the S3P phosphorus when bound to the isolated domain is very similar to that of S3P bound to EPSP synthase. We also conclude that most of the free energy of S3P binding to EPSP synthase is contributed by the N-terminal domain.
机译：5-Eno1pyruvylshikimate-3-PhosPhate（EPSP）合酶催化烯醇丙酮酸部分从磷酸烯醇丙酮酸（PEP）转移至sh草酸酯-3-磷酸酯（S3P）。诱变和X射线晶体学数据表明，该酶的活性位点位于其两个球状结构域之间的缝隙中。然而，他们还没有定义哪些残基负责底物的结合和催化。在这里，我们尝试结合使用核磁共振波谱法和等温滴定量热法，将底物S3P与EPSP合酶分离的N末端域结合。我们的实验结果表明，在S3P结合后，分离的N末端结构域中存在可饱和且稳定的构象变化，并且当与分离的结构域结合时，S3P磷的化学环境与与EPSP合酶结合的S3P的化学环境非常相似。我们还得出结论，S3P与EPSP合酶结合的大部分自由能是由N末端域贡献的。

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