2-(2-furyl)propan-1-yl acetate | 445399-65-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 杂芳族化合物
• 英文名称: 2-(2-furyl)propan-1-yl acetate
• 英文别名: 2-(Furan-2-yl)propyl acetate；2-(furan-2-yl)propyl acetate
• CAS: 445399-65-5
• 化学式: C₉H₁₂O₃
• 分子量: 168.192
• InChiKey: ZCUDEBDFUHJMJF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  12
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  39.4
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-(2-furyl)propan-1-yl acetate 在 Porcine Pancreas Lipase 、 silica gel 、 potassium carbonate 作用下， 以 甲醇 、 phosphate buffer 、 二甲基亚砜 为溶剂， 反应 4.0h， 生成 (2S)-2-(furan-2-yl)propan-1-ol
  参考文献：
  名称：

  Enzymatic kinetic resolution of 1-(3′-furyl)-3-buten-1-ol and 2-(2′-furyl)-propan-1-ol

  摘要：

  The enzymatic kinetic resolution of the racemic alcohols 1-(3'-furyl)-3-buten-1-ol(+/-)-1 and 2-(2'-furyl)propan-1-ol (+/-)-2 was investigated by screening a range of lipases and esterases for enantioselective transacylation, as well as for enantioselective hydrolysis. For both alcohols, lipase-catalyzed hydrolysis of the derived racemic acetate gave the best results for accessing the desired (S)-enantiomers. In the case of the secondary alcohol (+/-)-1 ASL turned out to be the optimum enzyme, whereas PPL was found to be superior in the case of the primary alcohol (+/-)-2. Additionally, an alternative access to (S)-2 via Oppolzer's camphor sultam methodology is described. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(02)00023-x
• 作为产物：
  描述：

  2-丙-1-烯-2-基呋喃 在 4-二甲氨基吡啶 、 硼烷 作用下， 以 四氢呋喃 、 吡啶 为溶剂， 反应 2.75h， 生成 2-(2-furyl)propan-1-yl acetate
  参考文献：
  名称：

  Enzymatic kinetic resolution of 1-(3′-furyl)-3-buten-1-ol and 2-(2′-furyl)-propan-1-ol

  摘要：

  The enzymatic kinetic resolution of the racemic alcohols 1-(3'-furyl)-3-buten-1-ol(+/-)-1 and 2-(2'-furyl)propan-1-ol (+/-)-2 was investigated by screening a range of lipases and esterases for enantioselective transacylation, as well as for enantioselective hydrolysis. For both alcohols, lipase-catalyzed hydrolysis of the derived racemic acetate gave the best results for accessing the desired (S)-enantiomers. In the case of the secondary alcohol (+/-)-1 ASL turned out to be the optimum enzyme, whereas PPL was found to be superior in the case of the primary alcohol (+/-)-2. Additionally, an alternative access to (S)-2 via Oppolzer's camphor sultam methodology is described. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(02)00023-x