(4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium iodide | 1305228-08-3

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium iodide
• CAS: 1305228-08-3
• 化学式: C₁₄H₂₄N*I
• 分子量: 333.256
• InChiKey: FBNBXNCVFCRATG-DSHXVJGRSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  0.25
• 重原子数：
  16.0
• 可旋转键数：
  1.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  3.01
• 氢给体数：
  0.0
• 氢受体数：
  0.0

反应信息

• 作为反应物：
  描述：

  (4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium iodide 在 sodium hydroxide 作用下， 以 氘代氯仿 、 水 为溶剂， 反应 1.0h， 生成 (4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium 2,2,2-trifluoroacetate
  参考文献：
  名称：

  Inhibition of (+)-Aristolochene Synthase with Iminium Salts Resembling Eudesmane Cation

  摘要：

  Trigonal iminium halides of (4aS,7S)-1,4a-dimethyl- and (4aS,7S)-4a-methyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium ions, aimed to mimic transition states associated with the aristolochene synthase-catalyzed cyclization of (-)-germacrene A to eudesmane cation, were evaluated under standard kinetic steady-state conditions. In the presence of inorganic diphosphate, these analogues were shown to competitively inhibit the enzyme, suggesting a stabilizing role for the diphosphate leaving group in this apparently endothermic transformation.

  DOI：

  10.1021/ol2000843
• 作为产物：
  描述：

  (4aS,7S)-4a-methyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium chloride 在 sodium hydroxide 作用下， 以 水 为溶剂， 反应 4.0h， 生成 (4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium iodide
  参考文献：
  名称：

  Inhibition of (+)-Aristolochene Synthase with Iminium Salts Resembling Eudesmane Cation

  摘要：

  Trigonal iminium halides of (4aS,7S)-1,4a-dimethyl- and (4aS,7S)-4a-methyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium ions, aimed to mimic transition states associated with the aristolochene synthase-catalyzed cyclization of (-)-germacrene A to eudesmane cation, were evaluated under standard kinetic steady-state conditions. In the presence of inorganic diphosphate, these analogues were shown to competitively inhibit the enzyme, suggesting a stabilizing role for the diphosphate leaving group in this apparently endothermic transformation.

  DOI：

  10.1021/ol2000843