(+/-)-2-phenoxy-1-propyl acetate | 71159-33-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: (+/-)-2-phenoxy-1-propyl acetate
• 英文别名: 2-phenoxy-1-propanol acetate；2-Phenoxypropyl acetate
• CAS: 71159-33-6
• 化学式: C₁₁H₁₄O₃
• 分子量: 194.23
• InChiKey: SHFZEARATMCIHW-UHFFFAOYSA-N

物化性质

• 沸点：
  255.7±13.0 °C(Predicted)
• 密度：
  1.059±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  14
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  35.5
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (+/-)-2-phenoxy-1-propyl acetate 在 Pseudomonas cepacia lipase 作用下， 以 aq. phosphate buffer 、 异丙醇 为溶剂， 生成 (S)-2-甲基-2-苯氧基甲醇
  参考文献：
  名称：

  A new mechanism of enantioselectivity toward chiral primary alcohol by lipase from Pseudomonas cepacia

  摘要：

  The stereo-recognition of chiral primary alcohols by lipase from Pseudomonas cepacia was found to deviate from earlier observations. Enantioselectivity toward 14 pairs of chiral primary alcohol esters by this lipase was dependent on the existence of an Onon-alpha (oxygen at non-alpha-position of the acyloxy group) in the alcohol moiety, and decreased as the size of the acyl moiety increased. Chemical modification on the lipase and molecular dynamics simulations indicated that Tyr(29) located within the catalytic cavity forms a hydrogen bond with the Onon-alpha of the preferred enantiomer of the primary alcohol ester. However, a larger acyl moiety suffered stronger hindrance from the catalytic cavity wall of the lipase, pushing the Onon-alpha away from Tyr(29), and thus weakening the stereo-recognition. (C) 2014 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2014.08.014
• 作为产物：
  描述：

  2-苯氧基丙酸 在 吡啶 、 硼烷 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 生成 (+/-)-2-phenoxy-1-propyl acetate
  参考文献：
  名称：

  Resolution of 2-aryloxy-1-propanols via lipase-catalyzed enantioselective acylation in organic media

  摘要：

  2-Aryloxy-1-propanols, primary alcohols with an oxygyen atom at the stereocenter. were resolved with good to high enantioselectivity by acylation with vinyl butanoate mediated by Pseudomonas sp. lipase in di-iso-propyl ether. Potential factors affecting the enantioselectivity of the enzymatic acylation were examined: solvents. acyl donors mid temperature, Using this enantioselective acylation procedure. enantiomeriocally pure (R)-2-(4-chlorophenoxy)-1-propanol was prepared on a grain scale. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(01)00258-0

文献信息

• Highly enantioselective kinetic resolution of primary alcohols of the type Ph-X-CH(CH3)-CH2OH by Pseudomonas cepacia lipase: effect of acyl chain length and solvent
  作者：Alessandra Mezzetti、Curtis Keith、Romas J. Kazlauskas

  DOI：10.1016/j.tetasy.2003.09.049

  日期：2003.12

  Although lipase from Pseudomonas cepacia (PCL) shows high enantioselectivity towards many secondary alcohols, it usually exhibits only low to moderate enantioselectivity towards primary alcohols. To increase this enantioselectivity, we optimised the reaction conditions for the PCL-catalysed hydrolysis of esters of three chiral primary alcohols: 2-methyl-3-phenyl-1-propanol 1, 2-phenoxy-1-propanol 2 and solketal 3. The enantioselectivity towards 1-acetate increased from E=16 to 38 upon changing the solvent from ethyl ether/phosphate buffer to 30% n-propanol in phosphate buffer and increased again to E greater than or equal to 190 upon changing the substrate from 1-acetate to 1-heptanoate. The same changes increased the enantioselectivity towards alcohol 2 from E=17 to 70, but did not significantly increase the enantioselectivity towards alcohol 3. The best solvent was similar to the solvent used to crystallise the open form of PCL and likely stabilises the open form of PCL. This stabilisation may increase the enantioselectivity by removing kinetic contributions from a non-enantioselective lid-opening step. We determined the kinetic contribution of the lid-opening step by measuring the interfacial activation of PCL. The activation energy for the PCL-catalysed hydrolysis of ethyl acetate was at least 2.6 kcal/mol lower in the presence of a water-organic solvent interface. (C) 2003 Elsevier Ltd. All rights reserved.
• Molecular Basis for Enantioselectivity of Lipase from <i>Pseudomonas cepacia</i> toward Primary Alcohols. Modeling, Kinetics, and Chemical Modification of Tyr29 to Increase or Decrease Enantioselectivity
  作者：W. Victor Tuomi、Romas J. Kazlauskas

  DOI：10.1021/jo981783y

  日期：1999.4.1

  Lipase from Pseudomonas cepacia (PCL) shows good enantioselectivity toward primary alcohols, An empirical rule can predict which enantiomer of a primary alcohol reacts faster, but there is no reliable strategy to increase the enantioselectivity. We used a combination of molecular modeling of lipase-transition state analogue complexes and kinetic measurements to identify the molecular basis of the enantioselectivity toward two primary alcohols: 2-methyl-3-phenyl-1-propanol, 1, and 2-phenoxy-1-propanol, 2. In hydrolysis of the acetate esters, PCL favors the (S)-enantiomer of both substrates (E = 16 and 17, respectively), but, due to changes in priorities of the substituents, the (S)-enantiomers of 1 and 2 have opposite shapes. Computer modeling of transition state analogues bound to PCL show that primary alcohols bind to PCL differently than secondary alcohols. Modeling and kinetics suggest that the enantioselectivity of PCL toward 1 comes from the binding of the methyl group at the stereocenter within a hydrophobic pocket for the fast-reacting enantiomer, but not for the slow-reacting enantiomer. On the other hand, the enantioselectivity toward 2 comes from an extra hydrogen bond between the phenoxy oxygen of the substrate to the phenolic OH of Tyr29. This hydrogen bond may slow release of the (R)-alcohol and thus account for the reversal of enantioselectvity. To decrease the enantioselectivity of PCL toward 2-acetate by a factor of 2 to E = 8, we eliminated the hydrogen bond by acetylation of the tyrosyl residues with N-acetylimidazole. To increase the enantioselectivity of PCL toward 2-acetate by a factor of 2 to E = 36, we increased the strength of the hydrogen bond by nitration of the tyrosyl residues with tetranitromethane. This is one of the first examples of a rationally designed modification of a lipase to increase enantioselectivity.