ethyl (2Z,4E)-6-[(tert-butyldiphenylsilyl)oxy]-2-fluoro-4-methylhexa-2,4-dienoate | 864971-49-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: ethyl (2Z,4E)-6-[(tert-butyldiphenylsilyl)oxy]-2-fluoro-4-methylhexa-2,4-dienoate
• CAS: 864971-49-3
• 化学式: C₂₅H₃₁FO₃Si
• 分子量: 426.603
• InChiKey: CNGXWJDZPQCPFC-LFHMYXRFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.93
• 重原子数：
  30.0
• 可旋转键数：
  8.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  35.53
• 氢给体数：
  0.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  ethyl (2Z,4E)-6-[(tert-butyldiphenylsilyl)oxy]-2-fluoro-4-methylhexa-2,4-dienoate 在 正丁基锂 、 barium permanganate 、 二异丁基氢化铝 作用下， 以 四氢呋喃 、 正己烷 、 二氯甲烷 为溶剂， 反应 16.5h， 生成 (7E,9Z,11Z,13E)-11-fluoro-all-trans-retinol
  参考文献：
  名称：

  On the mechanism of isomerization of all-trans-retinol esters to 11-cis-retinol in retinal pigment epithelial cells: 11-Fluoro-all-trans-retinol as substrate/inhibitor in the visual cycle

  摘要：

  The synthesis of 11-fluoro-all-trans-retinol (11-F-tROL), which is shown to be an excellent substrate for processing by visual cycle enzymes, is described. It is isomerized to its 11-cis congener subsequent to its esterification by lecithin retinol acyl transferase (LRAT) approximately as well as is vitamin A itself. The enzymatic turnover of 11-F-tROL is unaccompanied by enzyme inhibition. The previously reported lack of isomerization of this substrate had been suggested as evidence for a carbonium mechanism in the critical enzymatic isomerization pathway in vision. The mechanism of this process remains unknown. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2005.05.001
• 作为产物：
  描述：

  (ethoxycarbonylfluoromethyl)triphenylphosphonium bromide 、 (E)-4-((tert-butyldiphenylsilyl)oxy)-2-methylbut-2-enal 在 正丁基锂 作用下， 以 正己烷 、 二氯甲烷 为溶剂， 反应 2.83h， 以72%的产率得到ethyl (2Z,4E)-6-[(tert-butyldiphenylsilyl)oxy]-2-fluoro-4-methylhexa-2,4-dienoate
  参考文献：
  名称：

  On the mechanism of isomerization of all-trans-retinol esters to 11-cis-retinol in retinal pigment epithelial cells: 11-Fluoro-all-trans-retinol as substrate/inhibitor in the visual cycle

  摘要：

  The synthesis of 11-fluoro-all-trans-retinol (11-F-tROL), which is shown to be an excellent substrate for processing by visual cycle enzymes, is described. It is isomerized to its 11-cis congener subsequent to its esterification by lecithin retinol acyl transferase (LRAT) approximately as well as is vitamin A itself. The enzymatic turnover of 11-F-tROL is unaccompanied by enzyme inhibition. The previously reported lack of isomerization of this substrate had been suggested as evidence for a carbonium mechanism in the critical enzymatic isomerization pathway in vision. The mechanism of this process remains unknown. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2005.05.001