1,3-bis<3-(6-chloro-5-nitrouracilyl)>propane | 228396-44-9

• 分子结构分类: 有机化合物 - 有机1,3-偶极化合物 - 烯丙基型1,3-偶极有机化合物
• 英文名称: 1,3-bis<3-(6-chloro-5-nitrouracilyl)>propane
• 英文别名: 6-chloro-3-[3-(6-chloro-5-nitro-2,4-dioxo-1H-pyrimidin-3-yl)propyl]-5-nitro-1H-pyrimidine-2,4-dione
• CAS: 228396-44-9
• 化学式: C₁₁H₈Cl₂N₆O₈
• 分子量: 423.126
• InChiKey: WNRVMTPFFZPRKJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  27
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  191
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  1,3-bis<3-(6-chloro-5-nitrouracilyl)>propane 在 palladium on activated charcoal 盐酸 、 氢气 作用下， 以 乙醇 、 水 为溶剂， 反应 38.0h， 生成 1,3-bis<3-(6,7-dimethyl-8-D-ribityllumazinyl)>propane
  参考文献：
  名称：

  Synthesis and Biochemical Evaluation of Bis(6,7-dimethyl-8-d-ribityllumazines) as Potential Bisubstrate Analogue Inhibitors of Riboflavin Synthase

  摘要：

  The reaction catalyzed by riboflavin synthase utilizes two identical 6,7-dimethyl-8-n-ribityllumazine substrate molecules. Three bis(6,7-dimethyl-8-D-ribityllumazines) were, therefore, synthesized in which the two lumazine moieties were connected through their N-3 nitrogen atoms by polymethylene linker chains containing three, four, and five carbon atoms. The compounds with three and five carbon linkers were found to be very weak inhibitors of riboflavin synthase, having inhibition constants of 320 and >1000 mu M, respectively. In contrast, the bis(lumazine) with a four-carbon linker was much more potent, with an inhibition constant of 37 mu M. These results have potential implications for understanding the distance between the donor and acceptor sites of riboflavin synthase and the orientations of the two 6,7-dimethyl-8-D-ribityllumazine substrate molecules which occupy these two sites.

  DOI：

  10.1021/jo9821731
• 作为产物：
  描述：

  1,3-bis<3-(1-methoxymethyl-6-chlorouracilyl)>propane 在 硫酸 、 硝酸 作用下， 反应 0.5h， 以91%的产率得到1,3-bis<3-(6-chloro-5-nitrouracilyl)>propane
  参考文献：
  名称：

  Synthesis and Biochemical Evaluation of Bis(6,7-dimethyl-8-d-ribityllumazines) as Potential Bisubstrate Analogue Inhibitors of Riboflavin Synthase

  摘要：

  The reaction catalyzed by riboflavin synthase utilizes two identical 6,7-dimethyl-8-n-ribityllumazine substrate molecules. Three bis(6,7-dimethyl-8-D-ribityllumazines) were, therefore, synthesized in which the two lumazine moieties were connected through their N-3 nitrogen atoms by polymethylene linker chains containing three, four, and five carbon atoms. The compounds with three and five carbon linkers were found to be very weak inhibitors of riboflavin synthase, having inhibition constants of 320 and >1000 mu M, respectively. In contrast, the bis(lumazine) with a four-carbon linker was much more potent, with an inhibition constant of 37 mu M. These results have potential implications for understanding the distance between the donor and acceptor sites of riboflavin synthase and the orientations of the two 6,7-dimethyl-8-D-ribityllumazine substrate molecules which occupy these two sites.

  DOI：

  10.1021/jo9821731

文献信息

• Synthesis and Biochemical Evaluation of Bis(6,7-dimethyl-8-<scp>d</scp>-ribityllumazines) as Potential Bisubstrate Analogue Inhibitors of Riboflavin Synthase
  作者：Mark Cushman、Farahnaz Mavandadi、Donglai Yang、Karl Kugelbrey、Klaus Kis、Adelbert Bacher

  DOI：10.1021/jo9821731

  日期：1999.6.1

  The reaction catalyzed by riboflavin synthase utilizes two identical 6,7-dimethyl-8-n-ribityllumazine substrate molecules. Three bis(6,7-dimethyl-8-D-ribityllumazines) were, therefore, synthesized in which the two lumazine moieties were connected through their N-3 nitrogen atoms by polymethylene linker chains containing three, four, and five carbon atoms. The compounds with three and five carbon linkers were found to be very weak inhibitors of riboflavin synthase, having inhibition constants of 320 and >1000 mu M, respectively. In contrast, the bis(lumazine) with a four-carbon linker was much more potent, with an inhibition constant of 37 mu M. These results have potential implications for understanding the distance between the donor and acceptor sites of riboflavin synthase and the orientations of the two 6,7-dimethyl-8-D-ribityllumazine substrate molecules which occupy these two sites.