2-乙酰氨基-3-苯基丙酸丁酯 | 2361-98-0

• 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
• 中文名称: 2-乙酰氨基-3-苯基丙酸丁酯
• 英文名称: butyl 2-acetylamino-3-phenylpropanoate
• 英文别名: S-N-acetylphenylalanine butyl ester；butyl (2S)-2-acetamido-3-phenylpropanoate
• CAS: 2361-98-0
• 化学式: C₁₅H₂₁NO₃
• 分子量: 263.337
• InChiKey: SURCSYZOBGEWTF-AWEZNQCLSA-N

物化性质

• 沸点：
  425.4±33.0 °C(Predicted)
• 密度：
  1.063±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  19
• 可旋转键数：
  8
• 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
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  (E)-2-Acetylamino-3-phenyl-acrylic acid butyl ester 在 ClO4 、 氢气 作用下， 以 甲醇 为溶剂， 50.0 ℃ 、101.32 kPa 条件下， 反应 1.0h， 生成 2-乙酰氨基-3-苯基丙酸丁酯
  参考文献：
  名称：

  Asymmetric hydrogenation in the presence of bisdiphenylphosphine complexes op rhodium. 3. Molecular structure of 2R-3-PHENYL-2-(N-methyldiphenylphosphinamino)-1-diphenylphosphinoxypropane (1,5-cyclooctadiene)rhodium(I) perchlorate and its effectiveness as an enantioselective catalyst

  摘要：

  DOI：

  10.1007/bf00955817

文献信息

• Homogeneous enzymatic reactions in ionic liquids with poly(ethylene glycol)-modified subtilisin
  作者：Kazunori Nakashima、Tatsuo Maruyama、Noriho Kamiya、Masahiro Goto

  DOI：10.1039/b608920h

  日期：——

  Subtilisin Carlsberg was covalently modified with comb-shaped poly(ethylene glycol) (PM13). PM13-modified subtilisin (PM13-Sub) was readily solubilized in three different ionic liquids (ILs), i.e., [Emim][Tf2N], [C2OC1mim][Tf2N] and [C2OHmim][Tf2N]. Analysis of homogeneous enzymatic reactions in the ILs revealed that PM13-Sub exhibited excellent catalytic performance while the native enzyme suspended in ILs showed no activity. Hydrophobicity of ILs slightly affected enzyme activity, and the relatively hydrophobic IL [Emim][Tf2N] was the preferred medium for enzymatic reactions, similar to enzymatic reactions in conventional organic solvents. Enzyme activity was much higher in [Emim][Tf2N] than in conventional organic solvents, and excellent activity was associated with unique properties of ILs such as hydrophobicity and high polarity. Furthermore, PM13-Sub showed good stability in [Emim][Tf2N], and maintained 80% of its initial activity after 60 h.

  卡尔斯堡的类蛋白酶经过共价修饰，使用了梳状聚乙烯醇（PM13）。PM13修饰的类蛋白酶（PM13-Sub）能够在三种不同的离子液体（ILs）中良好溶解，即[Emim][Tf2N]、[C2OC1mim][Tf2N]和[C2OHmim][Tf2N]。在这些离子液体中进行的均相酶促反应分析显示，PM13-Sub表现出卓越的催化性能，而悬浮在离子液体中的天然酶则没有活性。离子液体的疏水性对酶活性有轻微影响，相对疏水性的离子液体[Emim][Tf2N]是酶促反应的优选介质，类似于传统有机溶剂中的酶促反应。在[Emim][Tf2N]中，酶活性远高于传统有机溶剂，且出色的活性与离子液体的独特性质，如疏水性和高极性密切相关。此外，PM13-Sub在[Emim][Tf2N]中表现出良好的稳定性，经过60小时后仍保持80%的初始活性。
• Asymmetric chemoenzymatic synthesis of N-acetyl-α-amino esters based on lipase-catalyzed kinetic resolutions through interesterification reactions
  作者：Marcos Reinaldo da Silva、Marcos Carlos de Mattos、Maria da Conceição Ferreira de Oliveira、Telma Leda Gomes de Lemos、Nágila Maria Pontes Silva Ricardo、Gonzalo de Gonzalo、Iván Lavandera、Vicente Gotor-Fernández、Vicente Gotor

  DOI：10.1016/j.tet.2014.02.012

  日期：2014.4

  transfer catalysts, this compound reacted with several alkyl halides, being benzyltributylammonium chloride identified as the best one for the production of a series of quaternary amino acids in moderate to excellent yields (52–95%). Then, the corresponding N-acetyl-phenylalanine methyl and allyl ester derivatives were obtained through acidic hydrolysis, esterification, and N-acetylation. Rhizomucor miehei

  从容易获得的乙酰氨基氰基乙酸乙酯开始，已经通过四步路线合成了几种苯丙氨酸类似物。在第一个反应中，并使用相转移催化剂，该化合物与几种烷基卤反应，即苄基三丁基氯化铵，被确定为以中等至极高产率（52–95％）生产一系列季氨基酸的最佳选择。然后，通过酸性水解，酯化和N-乙酰化获得相应的N-乙酰基-苯丙氨酸甲基和烯丙基酯衍生物。根瘤菌脂肪酶被认为是用于拆分这些氨基酯的通用酶，通过与丁酸丁酯在乙腈中进行酯交换反应获得最佳结果。发现取决于化合物的化学结构，对立体选择性有很大的影响，对于苯环中的未取代或对位取代，实现了极好的立体选择性，对间硝基衍生物适中，而邻硝基氨基酯则对中等选择性具有中等选择性。不反应。
• 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。
• Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting
  作者：Joyeeta Mukherjee、Munishwar N. Gupta

  DOI：10.1016/j.tetlet.2015.05.101

  日期：2015.7

  Bioimprinting is a technique in which an aqueous solution of a protein molecule along with the imprint molecule is dried to remove bulk water. Subtilisin was dissolved in an aqueous buffer with a substrate analog and precipitated with the substrate alcohol to obtain a dually bioimprinted enzyme precipitate. Precipitation was found to be a better bioimprinting technique than freeze drying used so far. The precipitation also enabled simultaneous bioimprinting with the alcohol substrate reinforcing the existing imprint with the substrate analog. The dually bioimprinted subtilisin was found out to be 65-fold more efficient than the freeze dried non-imprinted powder of subtilisin and could transesterify N-acetyl-tphenylalanine with n-propanol up to 82% in 5 h. (c) 2015 Elsevier Ltd. All rights reserved.
• Method of producing L-phenylalanine
  申请人：KURARAY CO., LTD.

  公开号：EP0198397B1

  公开（公告）日：1993-01-07