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首页> 外文期刊>Organic letters >Study of 1-Deoxy-D-xylulose-5-phosphate Reductoisomerase:Synthesis and Evaluation of Fluorinated Substrate Analogues
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Study of 1-Deoxy-D-xylulose-5-phosphate Reductoisomerase:Synthesis and Evaluation of Fluorinated Substrate Analogues

机译:1-脱氧-D-木酮糖-5-磷酸还原异构酶的研究:氟化底物类似物的合成与评价

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摘要

1-Deoxy-D-xylulose-5-phosphate(DXP)reductoisomerase is a NADPH-dependent enzyme catalyzing the conversion of DXP to methyl-o-erythritol 4-phosphate(MEP).In this study,each of the hydroxyl groups in DXP and one of its C-1 hydrogen atoms,were separately replaced with a fluorine atom and the effect of the substitution on the catalytic turnover was examined.It was found that the 1-fluoro-DXP is a poor substrate,while both 3-and 4-fluoro-DXP behave as noncompetitive inhibitors.
机译:1-脱氧-D-木酮糖-5-磷酸(DXP)还原异构酶是NADPH依赖性酶,催化DXP转化为甲基-邻-赤藓糖醇4-磷酸(MEP)。在本研究中,DXP中的每个羟基然后将其C-1氢原子之一分别替换为氟原子,并研究了取代基对催化转换的影响。发现1-氟-DXP是较差的底物,而3-和DXP 4-氟-DXP具有非竞争性抑制剂的作用。

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