5-(6-chloro-2,4-dihydroxypyrimidin-5-yl)pentan-1-sulfonic acid | 225652-45-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 5-(6-chloro-2,4-dihydroxypyrimidin-5-yl)pentan-1-sulfonic acid
• 英文别名: 5-(6-chloro-2,4-dioxo-1H-pyrimidin-5-yl)pentane-1-sulfonic acid
• CAS: 225652-45-9
• 化学式: C₉H₁₃ClN₂O₅S
• 分子量: 296.732
• InChiKey: VEDQRHWJTOMWSP-UHFFFAOYSA-N

物化性质

• 密度：
  1.560±0.10 g/cm3(Temp: 25 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  18
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  121
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  D-Ribamin 、 5-(6-chloro-2,4-dihydroxypyrimidin-5-yl)pentan-1-sulfonic acid 以 乙二醇甲醚 为溶剂， 反应 23.0h， 以27%的产率得到5-(6-D-ribitylamino-2,4-dihydroxypyrimidin-5-yl)pentane-1-sulfonic acid
  参考文献：
  名称：

  Design, Synthesis, and Biological Evaluation of Homologous Phosphonic Acids and Sulfonic Acids as Inhibitors of Lumazine Synthase

  摘要：

  Three phosphonic acid inhibitors of lumazine synthase were synthesized in which the phosphorus atom was separated from the pyrimidinedione ring by polymethylene linker chains containing four, five, and six carbon atoms. Three analogous sulfonic acids were also synthesized. The inhibitors were designed as metabolically stable analogues of a hypothetical intermediate in the reaction catalyzed by lumazine synthase, and the design process was supported by the results of computer graphics molecular modeling of the inhibitors within the active site of the enzyme. The most potent of the new inhibitors, 6-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-hexylphosphonic acid, inhibited recombinant lumazine synthase beta(60) capsids of Bacillus subtilis with a K-i of 130 mu M, making it the most potent inhibitor of lumazine synthase reported to date.

  DOI：

  10.1021/jo9821729
• 作为产物：
  描述：

  5-(6-chloro-2,4-dimethoxypyrimidin-5-yl)pentan-1-sulfonic acid sodium salt 在 盐酸 作用下， 以 水 、 溶剂黄146 为溶剂， 反应 2.5h， 以81%的产率得到5-(6-chloro-2,4-dihydroxypyrimidin-5-yl)pentan-1-sulfonic acid
  参考文献：
  名称：

  Design, Synthesis, and Biological Evaluation of Homologous Phosphonic Acids and Sulfonic Acids as Inhibitors of Lumazine Synthase

  摘要：

  Three phosphonic acid inhibitors of lumazine synthase were synthesized in which the phosphorus atom was separated from the pyrimidinedione ring by polymethylene linker chains containing four, five, and six carbon atoms. Three analogous sulfonic acids were also synthesized. The inhibitors were designed as metabolically stable analogues of a hypothetical intermediate in the reaction catalyzed by lumazine synthase, and the design process was supported by the results of computer graphics molecular modeling of the inhibitors within the active site of the enzyme. The most potent of the new inhibitors, 6-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-hexylphosphonic acid, inhibited recombinant lumazine synthase beta(60) capsids of Bacillus subtilis with a K-i of 130 mu M, making it the most potent inhibitor of lumazine synthase reported to date.

  DOI：

  10.1021/jo9821729

文献信息

• Design, Synthesis, and Biological Evaluation of Homologous Phosphonic Acids and Sulfonic Acids as Inhibitors of Lumazine Synthase
  作者：Mark Cushman、Jeffrey T. Mihalic、Klaus Kis、Adelbert Bacher

  DOI：10.1021/jo9821729

  日期：1999.5.1

  Three phosphonic acid inhibitors of lumazine synthase were synthesized in which the phosphorus atom was separated from the pyrimidinedione ring by polymethylene linker chains containing four, five, and six carbon atoms. Three analogous sulfonic acids were also synthesized. The inhibitors were designed as metabolically stable analogues of a hypothetical intermediate in the reaction catalyzed by lumazine synthase, and the design process was supported by the results of computer graphics molecular modeling of the inhibitors within the active site of the enzyme. The most potent of the new inhibitors, 6-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-hexylphosphonic acid, inhibited recombinant lumazine synthase beta(60) capsids of Bacillus subtilis with a K-i of 130 mu M, making it the most potent inhibitor of lumazine synthase reported to date.