| 1334218-06-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• CAS: 1334218-06-2
• 化学式: C₁₉H₃₈O₉P₂
• 分子量: 472.453
• InChiKey: IFSWNTADTQESRM-FBMGVBCBSA-N

物化性质

• 沸点：
  538.9±50.0 °C(predicted)
• 密度：
  1.126±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.85
• 重原子数：
  30.0
• 可旋转键数：
  18.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.84
• 拓扑面积：
  106.59
• 氢给体数：
  0.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  三甲基溴硅烷 、 在 甲醇 作用下， 以 二氯甲烷 为溶剂， 生成 、
  参考文献：
  名称：

  Synthesis and evaluation of dual site inhibitors of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase

  摘要：

  3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the first step of the shikimate pathway for the biosynthesis of aromatic compounds. Enzymes of this pathway have been identified as potential targets for drug design. The reaction catalysed by DAH7P synthase is an aldol condensation between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P). In this study inhibitors of DAH7P synthase were prepared which were designed to fit into the binding sites of both PEP and E4P substrates simultaneously. Inhibitors, known to target the PEP binding site, were extended using a C4 linker to include an appropriately placed phosphate group in order to access the phosphate-binding site of E4P. A small increase in inhibition was observed with this modification, and the inhibition results have been rationalised by induced-fit docking. (c) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.03.071
• 作为产物：
  描述：

  5-(tert-butyldiphenylsilyloxy)pentanal 在 4-二甲氨基吡啶 、 正丁基锂 、 potassium isopropoxide 、 四丁基氟化铵 、 碘 、 sodium hydrogensulfite 、 magnesium 、 二异丙胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 乙醚 、 正己烷 、 二氯甲烷 、 水 、 异丙醇 、 甲苯 为溶剂， 反应 11.83h， 生成
  参考文献：
  名称：

  Synthesis and evaluation of dual site inhibitors of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase

  摘要：

  3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the first step of the shikimate pathway for the biosynthesis of aromatic compounds. Enzymes of this pathway have been identified as potential targets for drug design. The reaction catalysed by DAH7P synthase is an aldol condensation between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P). In this study inhibitors of DAH7P synthase were prepared which were designed to fit into the binding sites of both PEP and E4P substrates simultaneously. Inhibitors, known to target the PEP binding site, were extended using a C4 linker to include an appropriately placed phosphate group in order to access the phosphate-binding site of E4P. A small increase in inhibition was observed with this modification, and the inhibition results have been rationalised by induced-fit docking. (c) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.03.071