benzyl 2-bromo-2-(o-tolyl)acetate | 404928-10-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: benzyl 2-bromo-2-(o-tolyl)acetate
• 英文别名: benzyl (+/-)-2-bromo-o-tolyl-acetate；(+/-)-2-bromo-2-o-tolylacetic acid benzyl ester；benzyl 2-bromo-2-(2-methylphenyl)acetate
• CAS: 404928-10-5
• 化学式: C₁₆H₁₅BrO₂
• 分子量: 319.198
• InChiKey: UFGUZCUPWQGYPZ-UHFFFAOYSA-N

物化性质

• 沸点：
  390.0±32.0 °C(Predicted)
• 密度：
  1.369±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.5
• 重原子数：
  19
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  benzyl 2-bromo-2-(o-tolyl)acetate 在 水 作用下， 以 癸烷 为溶剂， 反应 1.33h， 生成 (S)-2-bromo-2-o-tolylacetic acid 、 (R)-2-bromo-2-(o-tolyl)acetic acid 、 benzyl (S)-2-bromo-2-(o-tolyl)acetate
  参考文献：
  名称：

  A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters

  摘要：

  A variant of Lip2p lipase from Yarrowia lipolytica yeast was used for the resolution of 2-bromophenyl and o-tolyl acid esters, an important class of chemical intermediates for the pharmaceutical industry. In comparison with wild-type Lip2p, this variant, which contains one single amino acid change in the active site of the enzyme, V232A, displayed an enantioselectivity enhanced by one order of magnitude for the resolution of 2-bromo-phenylacetic acid ethyl ester (E-value increased from 5.5 to 59 for wild-type and V232A, respectively) and by fourfold for the resolution of 2-bromo-o-tolylacetic acid ethyl ester (going from an E-value of 27 to 111 for the wild-type and V232A, respectively). A remarkable increase in reaction velocity was also observed for both compounds, as a result of a significant gain in reactivity towards the favoured (S)-enantiomer (3- and 16-fold increase for 2-bromo-phenylacetic and -o-tolylacetic acid ethyl esters, respectively). These results demonstrate the key role of the V232 amino acid in enantiomer recognition and selectivity. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2008.06.009
• 作为产物：
  描述：

  邻甲基苯乙酸 在 硫酸 、 氢溴酸 、 对甲苯磺酸 作用下， 以 水 为溶剂， 反应 3.0h， 生成 benzyl 2-bromo-2-(o-tolyl)acetate
  参考文献：
  名称：

  Resolution of 2-bromo-o-tolyl-carboxylic acid by transesterification using lipases from Rhizomucor miehei and Pseudomonas cepacia

  摘要：

  Several lipases were screened for their ability to catalyze the enantioselective transesterification of 2-bromo-o-tolyl acetic acid. Amongst the preparations tested, the lipases from Rhizomucor miehei and Pseudomonas cepacia were selected. The best enantioselectivity was obtained with Rhizomucor miehei lipase immobilized on polypropylene (E = 11.3), which was more stereoselective than the free form. Hydrophobic solvents with log P higher than 2.5 were the most suitable giving the highest E-values. In addition, factors such as the water activity and the reaction temperature had little effect on the resolution of the racemic mixture. The selectivity of the enzymes with respect to the substrate was also only weakly affected by the structure of the leaving alcohol except in the case of the iso-propyl group, which causes high steric hindrance. Operating conditions under reduced pressure were defined to resolve the racemic mixture with immobilized Rhizomucor miehei lipase. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(01)00432-3

文献信息

• Lipase-catalyzed enantioselective transesterification toward esters of 2-bromo-tolylacetic acids
  作者：David Guieysse、Christophe Salagnad、Pierre Monsan、Magali Remaud-Simeon

  DOI：10.1016/s0957-4166(02)00784-x

  日期：2003.2

  Lipases from Candida antarctica, Pseudomonas cepacia and Rhizomucor miehei were tested in the resolution of seven racemic substrates belonging to the (RS)-2-bromo tolyl acetate ester category, but differing either in the position of the methyl substituent on the acyl part of the aromatic ring, or in the structure of the alkyl group. Lipase-catalyzed kinetic resolution via transesterification reaction between the ester and octanol in octane revealed that, of the three enzymes tested, P. cepacia lipase is the most efficient for resolution of the various racemates, with R-enantiopreference. In addition, the position of the methyl substituent was found to play a key role in governing the enantioselectivity of the reaction. Using P. cepacia lipase and 2-bromo-in/p-tolyl- or 2-bromophenylacetic acid esters E-values of >50 were measured, whereas with the ortho derivatives, E-values dramatically decreased to <6. (C) 2003 Elsevier Science Ltd. All rights reserved.
• Resolution of 2-bromo-o-tolyl-carboxylic acid by transesterification using lipases from Rhizomucor miehei and Pseudomonas cepacia
  作者：David Guieysse、Christophe Salagnad、Pierre Monsan、Magali Remaud-Simeon

  DOI：10.1016/s0957-4166(01)00432-3

  日期：2001.9

  Several lipases were screened for their ability to catalyze the enantioselective transesterification of 2-bromo-o-tolyl acetic acid. Amongst the preparations tested, the lipases from Rhizomucor miehei and Pseudomonas cepacia were selected. The best enantioselectivity was obtained with Rhizomucor miehei lipase immobilized on polypropylene (E = 11.3), which was more stereoselective than the free form. Hydrophobic solvents with log P higher than 2.5 were the most suitable giving the highest E-values. In addition, factors such as the water activity and the reaction temperature had little effect on the resolution of the racemic mixture. The selectivity of the enzymes with respect to the substrate was also only weakly affected by the structure of the leaving alcohol except in the case of the iso-propyl group, which causes high steric hindrance. Operating conditions under reduced pressure were defined to resolve the racemic mixture with immobilized Rhizomucor miehei lipase. (C) 2001 Elsevier Science Ltd. All rights reserved.
• A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters
  作者：Miguel Cancino、Philippe Bauchart、Georgina Sandoval、Jean-Marc Nicaud、Isabelle André、Valérie Dossat、Alain Marty

  DOI：10.1016/j.tetasy.2008.06.009

  日期：2008.7

  A variant of Lip2p lipase from Yarrowia lipolytica yeast was used for the resolution of 2-bromophenyl and o-tolyl acid esters, an important class of chemical intermediates for the pharmaceutical industry. In comparison with wild-type Lip2p, this variant, which contains one single amino acid change in the active site of the enzyme, V232A, displayed an enantioselectivity enhanced by one order of magnitude for the resolution of 2-bromo-phenylacetic acid ethyl ester (E-value increased from 5.5 to 59 for wild-type and V232A, respectively) and by fourfold for the resolution of 2-bromo-o-tolylacetic acid ethyl ester (going from an E-value of 27 to 111 for the wild-type and V232A, respectively). A remarkable increase in reaction velocity was also observed for both compounds, as a result of a significant gain in reactivity towards the favoured (S)-enantiomer (3- and 16-fold increase for 2-bromo-phenylacetic and -o-tolylacetic acid ethyl esters, respectively). These results demonstrate the key role of the V232 amino acid in enantiomer recognition and selectivity. (C) 2008 Elsevier Ltd. All rights reserved.