(1R,2R,4S,5R)-(+)-4-hydroxy-6-oxabicyclo<3.1.0>hex-2-yl acetate | 247595-16-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 氧烷类
• 英文名称: (1R,2R,4S,5R)-(+)-4-hydroxy-6-oxabicyclo<3.1.0>hex-2-yl acetate
• 英文别名: (1S,2R,4S,5R)-(-)-2-Hydroxy-6-oxabicyclo<3.1.0>hex-4-yl acetate；[(1S,2R,4S,5R)-4-hydroxy-6-oxabicyclo[3.1.0]hexan-2-yl] acetate
• CAS: 247595-16-0
• 化学式: C₇H₁₀O₄
• 分子量: 158.154
• InChiKey: CIHXKEGIMFVUOV-WNJXEPBRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.55
• 重原子数：
  11.0
• 可旋转键数：
  1.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  59.06
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为产物：
  描述：

  (1R,3S)-(-)-1-乙酰氧基环戊烷-3-醇 在 四丁基氟化铵 、 碳酸氢钠 、 间氯过氧苯甲酸 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 0.5h， 生成 (1R,2R,4S,5R)-(+)-4-hydroxy-6-oxabicyclo<3.1.0>hex-2-yl acetate
  参考文献：
  名称：

  Lipase-catalyzed transesterification of meso-cyclopentane diols

  摘要：

  The lipase-catalyzed transesterification of the meso-cyclopentane diols 1a - 6a with vinyl acetate in tetrahydrofuran/triethylamine in the presence of lipases of different origin has been investigated. Depending on the structure of the substrate and the origin of the lipase chiral cyclopentane derivatives with high enantiomeric excess could be obtained in good to excellent chemical yields.

  DOI：

  10.1016/s0040-4020(01)88281-8

文献信息

• 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.