cis-3,5-di-iso-butyryloxycyclopent-1-ene | 161484-08-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: cis-3,5-di-iso-butyryloxycyclopent-1-ene
• 英文别名: cis-cyclopent-2-en-1,4-diyl diisobutyrate；(1R,3S)-cyclopent-4-ene-1,3-diyl bis(isobutyrate)；[(1S,4R)-4-(2-methylpropanoyloxy)cyclopent-2-en-1-yl] 2-methylpropanoate
• CAS: 161484-08-8
• 化学式: C₁₃H₂₀O₄
• 分子量: 240.299
• InChiKey: PKDQADQMMOJUKK-PHIMTYICSA-N

物化性质

• 沸点：
  289.341±40.00 °C(Press: 760.00 Torr)(predicted)
• 密度：
  1.059±0.10 g/cm3(Temp: 25 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  17
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  cis-3,5-di-iso-butyryloxycyclopent-1-ene 在 sodium dihydrogenphosphate 、 sodium azide 、 Electrophorus electricus acetylcholinesterase 作用下， 以48%的产率得到(1R,4S)-(+)-4-hydroxycyclopent-2-enyl isobutyrate
  参考文献：
  名称：

  Chiral induction in cyclopentyl-derived 1,3-meso-diesters: enantioselective hydrolyses with electric eel acetylcholinesterase

  摘要：

  Eight 1,3-meso-diesters derived from a common cyclopentyl backbone were exposed to the hydrolase enzyme acetylcholinesterase from Electrophorus electricus. All eight compounds were hydrolyzed by the enzyme. The overall enantioselectivities were quite high, and the resulting e.e.s were generally >90%. The absolute configurations of the product monoesters were determined through stereochemical correlation. These data revealed that the preferred site for enzymatic hydrolysis in seven of the substrates was the pro-S ester function, with pro-R cleavage detected in the eighth. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(99)00236-0
• 作为产物：
  描述：

  6-噁双环[3.1.0]-3-己烯 在 吡啶 、 四(三苯基膦)钯 作用下， 以 四氢呋喃 为溶剂， 反应 24.25h， 生成 cis-3,5-di-iso-butyryloxycyclopent-1-ene
  参考文献：
  名称：

  Chiral induction in cyclopentyl-derived 1,3-meso-diesters: enantioselective hydrolyses with electric eel acetylcholinesterase

  摘要：

  Eight 1,3-meso-diesters derived from a common cyclopentyl backbone were exposed to the hydrolase enzyme acetylcholinesterase from Electrophorus electricus. All eight compounds were hydrolyzed by the enzyme. The overall enantioselectivities were quite high, and the resulting e.e.s were generally >90%. The absolute configurations of the product monoesters were determined through stereochemical correlation. These data revealed that the preferred site for enzymatic hydrolysis in seven of the substrates was the pro-S ester function, with pro-R cleavage detected in the eighth. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(99)00236-0

文献信息

• Acylative Desymmetrization of Cyclic <i>meso</i>-1,3-Diols by Chiral DMAP Derivatives
  作者：Hiroki Mandai、Tsubasa Hironaka、Koichi Mitsudo、Seiji Suga

  DOI：10.1246/cl.200809

  日期：2021.3.5

  An efficient enantioselective acylative desymmetrization of cyclic meso-1,3-diols was developed by using a chiral DMAP derivative 1e having a 1,1′-binaphthyl unit. The reactions required only 0.5 m...

  通过使用具有 1,1'-联萘单元的手性 DMAP 衍生物 1e，开发了一种有效的环状内消旋 1,3-二醇的对映选择性酰化去对称化。反应只需要 0.5 m...
• 4-hydroxycyclopent-2-en-1-one and derivatives as chiral synthetic equivalents of cyclopentadienone in asymmetric diels-alder reactions
  作者：Paul P M.A. Dols、Antonius J.H. Klunder、Binne Zwanenburg

  DOI：10.1016/s0040-4020(01)85571-x

  日期：1994.1
• Chiral induction in cyclopentyl-derived 1,3-meso-diesters: enantioselective hydrolyses with electric eel acetylcholinesterase
  作者：Donald R Deardorff、Roberto B Amador、James W Morton、Henry Y Kim、Cullen M Taniguchi、Arnel A Balbuena、Sam A Warren、Vadim Fanous、S.W.Tina Choe

  DOI：10.1016/s0957-4166(99)00236-0

  日期：1999.6

  Eight 1,3-meso-diesters derived from a common cyclopentyl backbone were exposed to the hydrolase enzyme acetylcholinesterase from Electrophorus electricus. All eight compounds were hydrolyzed by the enzyme. The overall enantioselectivities were quite high, and the resulting e.e.s were generally >90%. The absolute configurations of the product monoesters were determined through stereochemical correlation. These data revealed that the preferred site for enzymatic hydrolysis in seven of the substrates was the pro-S ester function, with pro-R cleavage detected in the eighth. (C) 1999 Elsevier Science Ltd. All rights reserved.