N-acetyl-L-phenylalanine 2-octyl ester | 52126-16-6

• 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-octyl ester
• 英文别名: [(2S)-octan-2-yl] (2S)-2-acetamido-3-phenylpropanoate
• CAS: 52126-16-6
• 化学式: C₁₉H₂₉NO₃
• 分子量: 319.444
• InChiKey: AGDSCUFPXMGLQU-YJBOKZPZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  23
• 可旋转键数：
  11
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.58
• 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：

  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-octyl 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

• The Specificity of the Nucleophilic Site of α-Chymotrypsin and its Potential for the Resolution of Alcohols. Enzyme-catalyzed Hydrolyses of Some (+)-, (−)-, and (±)-2-Butyl, -2-Octyl, and -α-Phenethyl Esters
  作者：Yong Yeng Lin、David N. Palmer、J. Bryan Jones

  DOI：10.1139/v74-075

  日期：1974.2.1

  The α-chymotrypsin-catalyzed hydrolyses of a representative spectrum of (R)- and (S)-2-butyl, -2-octyl, and -α-phenethyl esters of N-acetyl-L-phenylalanine, N-acetylglycine, α-hydroxy-β-phenyl-propionic, dihydrocinnamic, and hippuric acids have been examined. The kinetic studies were carried out in order to provide data on the practicability of exploiting the stereospecificity of the nucleophilic region

  N-乙酰基-L-苯丙氨酸、N-乙酰基甘氨酸、α-(R)-和(S)-2-丁基、-2-辛基和-α-苯乙酯的代表性光谱的α-胰凝乳蛋白酶催化水解-羟基-β-苯基-丙酸、二氢肉桂酸和马尿酸已经过检测。进行动力学研究是为了提供关于利用酶活性位点亲核区域的立体特异性通过选择性水解外消旋醇的酯来拆分外消旋醇的可行性的数据。获得的数据表明醇部分的结构和手性影响底物的催化和结合常数，并且对于二氢肉桂酸酯和马尿酸盐系列的非特异性底物观察到对映体醇部分之间的最大差异。
• Chemically modified mutants of subtilisin Bacillus lentus catalyze transesterification reactions better than wild type
  作者：Michael Dickman、Richard C. Lloyd、J.Bryan Jones

  DOI：10.1016/s0957-4166(98)00450-9

  日期：1998.12

  mutagenesis and chemical modification strategy has been used to create superior enzyme catalysts for the resolution of racemic primary and secondary alcohols using a transesterification reaction. The chemically modified mutant, N62C–S–CH3, of subtilisin Bacillus lentus catalyzes the transesterification of N-acetyl-L-phenylalanine vinyl ester with β-branched primary alcohols faster than wild type. The

  结合使用了定点诱变和化学修饰策略，可通过酯交换反应创建出色的酶催化剂，用于拆分外消旋伯醇和仲醇。枯草杆菌蛋白酶芽孢杆菌的化学修饰突变体N62C–S–CH 3催化N-乙酰基-L-苯丙氨酸乙烯基酯与β-支化伯醇的酯交换反应比野生型更快。枯草杆菌蛋白酶芽孢杆菌的半胱氨酸突变体M222C的产率更高（1-苯基乙醇和2-辛醇的产率分别为98％和92％，而野生型为19％和10％），并且仲醇比野生型更好的对映选择性被使用。