3-(2-bromohexanoyloxy)-4-nitrobenzoic acid | 1357303-90-2

• 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: 3-(2-bromohexanoyloxy)-4-nitrobenzoic acid
• CAS: 1357303-90-2
• 化学式: C₁₃H₁₄BrNO₆
• 分子量: 360.161
• InChiKey: WVLPZMODRSBZGL-UHFFFAOYSA-N

物化性质

• 沸点：
  502.7±50.0 °C(Predicted)
• 密度：
  1.559±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.15
• 重原子数：
  21.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  106.74
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  3-(2-bromohexanoyloxy)-4-nitrobenzoic acid 在 N-甲基吗啉 、 三羟甲基氨基甲烷盐酸盐 、 sodium chloride 、 calcium chloride 、 氯甲酸异丁酯 作用下， 以 四氢呋喃 、 水 、 乙腈 为溶剂， 反应 96.5h， 生成 3-(2-methylhexanoyloxy)-4-nitrobenzoic acid
  参考文献：
  名称：

  Evaluation of snake venom phospholipase A2: hydrolysis of non-natural esters

  摘要：

  Phospholipase A(2) from the rattlesnake Crotalus durissus terrificus was employed for the first time to test its enantioseletivity on the hydrolysis of different non-natural esters. It was observed that the structure of this small enzyme is restrictive in the choice of its lipase action with non-natural substrates. Two forms of the enzyme were used; free and as its cross-linked enzyme aggregate (CLEA). With all substrates, the free enzyme showed activity similar to the CLEA preparation. The advantage of the CLEA phospholipase is the possibility to reuse it in several consecutive reactions without a decrease of activity and selectivity with good but higher yields and ee than with the free enzyme.

  DOI：

  10.1590/s0103-50532011000200016
• 作为产物：
  描述：

  2-溴己酰溴 、 3-羟基-4-硝基苯甲酸 在 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 生成 3-(2-bromohexanoyloxy)-4-nitrobenzoic acid
  参考文献：
  名称：

  Evaluation of snake venom phospholipase A2: hydrolysis of non-natural esters

  摘要：

  Phospholipase A(2) from the rattlesnake Crotalus durissus terrificus was employed for the first time to test its enantioseletivity on the hydrolysis of different non-natural esters. It was observed that the structure of this small enzyme is restrictive in the choice of its lipase action with non-natural substrates. Two forms of the enzyme were used; free and as its cross-linked enzyme aggregate (CLEA). With all substrates, the free enzyme showed activity similar to the CLEA preparation. The advantage of the CLEA phospholipase is the possibility to reuse it in several consecutive reactions without a decrease of activity and selectivity with good but higher yields and ee than with the free enzyme.

  DOI：

  10.1590/s0103-50532011000200016