N-acetyl-L-phenylalanine 2-butyl ester

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-acetyl-L-phenylalanine 2-butyl ester
• 英文别名: butan-2-yl (2S)-2-acetamido-3-phenylpropanoate
• 化学式: C₁₅H₂₁NO₃
• 分子量: 263.337
• InChiKey: ZDVMPCFPOZDRQL-IAXJKZSUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.08
• 重原子数：
  19.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  55.4
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为产物：
  描述：

  N-乙酰-L-苯丙氨酸 在 palladium diacetate 、 氢氧化钾 、 KCl-Subtilisin Bacillus lentus 作用下， 以 叔丁醇 为溶剂， 反应 96.0h， 生成 N-acetyl-L-phenylalanine 2-butyl ester
  参考文献：
  名称：

  Probing the specificity of the S 1 ′, leaving group, site of subtilisin Bacillus lentus using an enzyme-catalyzed transesterification reaction

  摘要：

  Subtilisin Bacillus lentus catalyzes transesterifications between N-acetyl-L-phenylalanine vinyl ester and a wide range of alcohols. Reaction yields are high when primary alcohols are used, and quantitative with methanol. With chiral alcohols, the reaction is enantioselective, and the stereoselectivity is reversed on going from open chain secondary alcohols to beta-branched primary alcohols. A model is proposed to account for this change in absolute configuration preference. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(98)00022-6

文献信息

• Solubilisation of α-chymotrypsin by hydrophobic ion pairing in fluorous systems and supercritical carbon dioxide and demonstration of efficient enzyme recycling
  作者：Karima Benaissi、Martyn Poliakoff、Neil R. Thomas

  DOI：10.1039/b904761a

  日期：——

  Hydrophobic ion-pairing (HIP) with the fluorinated surfactant KDP 4606 (KDP) was used to extract the protein α-chymotrypsin (CMT) into perfluoromethylcyclohexane (PFMC). The diameter of the solubilised CMT-KDP complexes formed in PFMC was determined by dynamic light scattering (DLS) to be 25 nm which suggested the formation of a protein aggregate containing ∼100 protein molecules surrounded by KDP 4606 surfactant molecules per particle. The catalytic activity of the protease CMT either solubilised by HIP or as the suspended native enzyme has been investigated in both a fluorous biphasic system (FBS) and a supercritical carbon dioxide (scCO2) batch reactor. Transesterification of N-acetyl-L-phenylalanine ethyl ester (APEE) with n-butanol or rac-2-butanol was catalysed by the protease in the FBS hexane-PFMC or scCO2 at 40 °C. Under comparable conditions, the amount of transesterification of the solubilised protease–surfactant (CMT-KDP) complex in PFMC (6–10%) was shown to be significantly higher than that of the suspended protease (1–3%) in either hexane–PFMC or scCO2. This suggested the formation of a catalytically active CMT-KDP aggregate in PFMC. The CMT-KDP complex which is retained in the fluorous phase on cooling the solution was successfully reused over four cycles with no loss of activity.

  利用疏水离子配对（HIP）与含氟表面活性剂KDP 4606（KDP）将蛋白质δ-糜蛋白酶（CMT）提取到全氟甲基环己烷（PFMC）中。通过动态光散射（DLS）测定，在PFMC中形成的增溶CMT-KDP复合物的直径为25纳米，这表明形成了一种蛋白质聚集体，每个颗粒含有¼100个蛋白质分子，周围环绕着KDP 4606表面活性剂分子。在氟双相系统（FBS）和超临界二氧化碳（scCO2）间歇反应器中研究了蛋白酶CMT的催化活性，无论是通过HIP溶解的蛋白酶还是悬浮的原生酶。蛋白酶在 40°C 的 FBS 己烷-PFMC 或 scCO2 中催化了 N-乙酰基-L-苯丙氨酸乙酯（APEE）与正丁醇或 rac-2 丁醇的酯交换反应。在可比条件下，PFMC 中溶解的蛋白酶与表面活性剂（CMT-KDP）复合物的酯交换量（6%-10%）明显高于正己烷-PFMC 或 scCO2 中悬浮蛋白酶的酯交换量（1%-3%）。这表明在 PFMC 中形成了具有催化活性的 CMT-KDP 聚集体。在冷却溶液时，CMT-KDP 复合物被保留在氟相中，该复合物被成功地重复使用了四个周期，且活性没有降低。