(R)-3-ethoxy-1-(furan-3-yl)-3-oxopropyl butyrate | 1312919-01-9

• 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: (R)-3-ethoxy-1-(furan-3-yl)-3-oxopropyl butyrate
• 英文别名: [(1R)-3-ethoxy-1-(furan-3-yl)-3-oxopropyl] butanoate
• CAS: 1312919-01-9
• 化学式: C₁₃H₁₈O₅
• 分子量: 254.283
• InChiKey: ZHWIBGCCCYLVMY-LLVKDONJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  18
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.54
• 拓扑面积：
  65.7
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  3-糠醛 在 divinylbenzene-crosslinked hydrophobic macroporous polymer-supported Candida antarctica lipase B 、 锌 作用下， 以 四氢呋喃 、 甲基叔丁基醚 为溶剂， 反应 62.0h， 生成 (S)-ethyl 3-(furan-3-yl)-3-hydroxypropanoate 、 (R)-3-ethoxy-1-(furan-3-yl)-3-oxopropyl butyrate
  参考文献：
  名称：

  Lipases A and B from Candida antarctica in the enantioselective acylation of ethyl 3-heteroaryl-3-hydroxypropanoates: aspects on the preparation and enantiopreference

  摘要：

  The preparative scale kinetic resolution of racemic ethyl 2- and 3-furyl- and 2- and 3-thienyl-3-hydroxypropanoates has been performed by Candida antarctica lipases A and B with vinyl esters. A study based on the present work together with the literature has been carried out in terms of lipase enantiopreference and substrate structure. We also discuss the excellent behavior of the lipase A in O-acylations of secondary alcohols with respect to enantiopreference. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2011.01.027

文献信息

• Lipases A and B from Candida antarctica in the enantioselective acylation of ethyl 3-heteroaryl-3-hydroxypropanoates: aspects on the preparation and enantiopreference
  作者：Jürgen Brem、Arto Liljeblad、Csaba Paizs、Monica Ioana Toşa、Florin-Dan Irimie、Liisa T. Kanerva

  DOI：10.1016/j.tetasy.2011.01.027

  日期：2011.2

  The preparative scale kinetic resolution of racemic ethyl 2- and 3-furyl- and 2- and 3-thienyl-3-hydroxypropanoates has been performed by Candida antarctica lipases A and B with vinyl esters. A study based on the present work together with the literature has been carried out in terms of lipase enantiopreference and substrate structure. We also discuss the excellent behavior of the lipase A in O-acylations of secondary alcohols with respect to enantiopreference. (C) 2011 Elsevier Ltd. All rights reserved.