2,2-bis(4-hydroxyphenyl)propane monohexanoate

• 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: 2,2-bis(4-hydroxyphenyl)propane monohexanoate
• 化学式: C₂₁H₂₆O₃
• 分子量: 326.436
• InChiKey: ILKAUWPCLFTATI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.2
• 重原子数：
  24.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  46.53
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  2,2-bis(4-hydroxyphenyl)propane monohexanoate 、 乙酸酐 在 4-二甲氨基吡啶 作用下， 以95%的产率得到2,2-bis(4-hydroxyphenyl)propane monohexanoate monoacetate
  参考文献：
  名称：

  Mapping the substrate selectivity and enantioselectivity of esterases from thermophiles

  摘要：

  To identify potential applications of nineteen esterases from thermophiles, we mapped their substrate selectivity and enantioselectivity using a library of 50 esters. We measured the selectivities colorimetrically using Quick E, which uses pH indicators to detect hydrolysis and a chromogenic reference compound as an internal control. The substrate selectivity mapping revealed one esterase, E018b, with a strong preference for acetyl esters (14- to 25-fold over hexanoate). The enantio selectivity mapping revealed a number of cases of high enantioselectivity. Thirteen of the 19 esterases showed moderate or better enantioselectivity (> 19) toward 1-phenethyl butyrate favoring the (R)-enantiomer and two esterases (E008, E013) showed moderate or better enantioselectivity (>20) toward methyl 2-chloropropionate favoring the (S)-enantiomer. Three esterases (E001, E004, E005) showed high (>46) enantioselectivity toward menthyl acetate favoring the (R)-enantiomer. This rapid mapping of the selectivity simplifies the characterization of new enzymes. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2004.07.044
• 作为产物：
  描述：

  双酚A 、 己酰氯 在 吡啶 作用下， 以 乙醚 为溶剂， 反应 2.0h， 以77%的产率得到2,2-bis(4-hydroxyphenyl)propane monohexanoate
  参考文献：
  名称：

  Mapping the substrate selectivity and enantioselectivity of esterases from thermophiles

  摘要：

  To identify potential applications of nineteen esterases from thermophiles, we mapped their substrate selectivity and enantioselectivity using a library of 50 esters. We measured the selectivities colorimetrically using Quick E, which uses pH indicators to detect hydrolysis and a chromogenic reference compound as an internal control. The substrate selectivity mapping revealed one esterase, E018b, with a strong preference for acetyl esters (14- to 25-fold over hexanoate). The enantio selectivity mapping revealed a number of cases of high enantioselectivity. Thirteen of the 19 esterases showed moderate or better enantioselectivity (> 19) toward 1-phenethyl butyrate favoring the (R)-enantiomer and two esterases (E008, E013) showed moderate or better enantioselectivity (>20) toward methyl 2-chloropropionate favoring the (S)-enantiomer. Three esterases (E001, E004, E005) showed high (>46) enantioselectivity toward menthyl acetate favoring the (R)-enantiomer. This rapid mapping of the selectivity simplifies the characterization of new enzymes. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2004.07.044

文献信息

• Mapping the substrate selectivity and enantioselectivity of esterases from thermophiles
  作者：Neil A. Somers、Romas J. Kazlauskas

  DOI：10.1016/j.tetasy.2004.07.044

  日期：2004.9

  To identify potential applications of nineteen esterases from thermophiles, we mapped their substrate selectivity and enantioselectivity using a library of 50 esters. We measured the selectivities colorimetrically using Quick E, which uses pH indicators to detect hydrolysis and a chromogenic reference compound as an internal control. The substrate selectivity mapping revealed one esterase, E018b, with a strong preference for acetyl esters (14- to 25-fold over hexanoate). The enantio selectivity mapping revealed a number of cases of high enantioselectivity. Thirteen of the 19 esterases showed moderate or better enantioselectivity (> 19) toward 1-phenethyl butyrate favoring the (R)-enantiomer and two esterases (E008, E013) showed moderate or better enantioselectivity (>20) toward methyl 2-chloropropionate favoring the (S)-enantiomer. Three esterases (E001, E004, E005) showed high (>46) enantioselectivity toward menthyl acetate favoring the (R)-enantiomer. This rapid mapping of the selectivity simplifies the characterization of new enzymes. (C) 2004 Elsevier Ltd. All rights reserved.