N-phenylacetyl aspartic acid | 2752-32-1

• 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-phenylacetyl aspartic acid
• 英文别名: N-phenylacetylaspartic acid；N-phenylacetylaspartate；N-benzylcarbonyl aspartic acid；N-Phenylacetyl-L-asparaginsaeure；(2-phenylacetyl)-L-aspartic acid；(2S)-2-[(2-phenylacetyl)amino]butanedioic acid
• CAS: 2752-32-1
• 化学式: C₁₂H₁₃NO₅
• 分子量: 251.239
• InChiKey: SVFKZPQPMMZHLZ-VIFPVBQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  18
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  104
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-phenylacetyl aspartic acid 以 9,10-蒽二基二(亚甲基)二乙酸酯 为溶剂， 反应 2.0h， 以70 g of N-phenylacetyl aspartic anhydride were obtained的产率得到N-phenylacetyl aspartic anhydride
  参考文献：
  名称：

  Process for preparing peptides

  摘要：

  该发明描述了一种制备肽的方法。更具体地，通过适当的N-酰基衍生物的酶解反应，描述和声明了一种制备L-.alpha.-天冬氨酸-L-苯丙氨酸C.sub.1-C.sub.4低烷基酯的方法。

  公开号：

  US04668625A1
• 作为产物：
  描述：

  (S)-dimethyl 2-(phenylacetamido)succinate 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 24.0h， 生成 N-phenylacetyl aspartic acid
  参考文献：
  名称：

  N-benzoylaspartate and N-phenylacetylaspartate from pea seeds

  摘要：

  DOI：

  10.1016/0031-9422(80)85147-8

文献信息

• Enzymic synthesis design and enzymic synthesis of aspartame
  作者：Ivanka B. Stoineva、Boris P. Galunsky、Valentin S. Lozanov、Ivailo P. Ivanov、Dimiter D. Petkov

  DOI：10.1016/s0040-4020(01)88207-7

  日期：1992.1

  An enzymic synthesis of aspartame (H-Asp-Phe-OMe) has been designed and realized based on the structure-activity study of thermolysin and penicillin amidase hydrolysis of its p-substituted phenylacetyl derivatives. These compounds meet the structural and energetic requirements of two enzymic binding sites The peptide sweetener has been prepared by thermolysin - catalyzed condensation of the p-substituted

  基于嗜热菌素和青霉素酰胺酶水解其对位取代的苯基乙酰基衍生物的结构活性研究，设计并实现了阿斯巴甜的酶促合成（H-Asp-Phe-OMe）。这些化合物满足两个酶结合位点的结构和能量要求。肽甜味剂的制备方法是：通过热解酶-对位取代的苯基乙酰基-Asp-OH和H-Phe-OMe的缩合反应，然后通过青霉素酰胺酶的催化，对所得产物进行脱保护。阿斯巴甜的前体。
• Method for purifying N-benzyloxycarbonyl aspartic acid
  申请人：PPG INDUSTRIES, INC.

  公开号：EP0072015A1

  公开（公告）日：1983-02-16

  N-benzyloxycarbonyl aspartic acid containing minor contaminating amounts of N-benzyloxycarbonyl aspartyl aspartic acid is purified by subjecting the impure material to alkaline hydrolysis at a pH of at least 10 and at temperatures of from 20°C. to 100°C., preferably 65°C. to 85°C., for a time sufficient to hydrolyze substantially all of the N-benzyloxycarbonyl aspartyl aspartic acid impurity therein. N-benzyloxycarbonyl aspartic acid containing less than 0.2 weight percent of the impurity can be obtained by such treatment.

  纯化含有少量 N-苄氧羰基天冬氨酸杂质的 N-苄氧羰基天冬氨酸的方法是将不纯物质在 pH 值至少为 10、温度为 20℃至 100℃、最好为 65℃至 85℃的条件下进行碱性水解，水解时间足以使其中的 N-苄氧羰基天冬氨酸杂质基本上全部水解。通过这种处理可以得到杂质含量小于 0.2 重量％的 N-苄氧羰基天冬氨酸。
• Verfahren zur Herstellung von Dipeptid-Additionsverbindungen und den daraus freigesetzten Dipeptiden
  申请人：HOECHST AKTIENGESELLSCHAFT

  公开号：EP0241864A2

  公开（公告）日：1987-10-21

  Bei der enzymatischen Verknüpfung von D-,L-Phenylalanin­alkylester oder L-Phenylalaninalkylester mit einer N-ge­schützten L-Asparaginsäure können eine Phenoxyacetyl-, Phenoxypropionyl- oder Phenylacetylgruppe als Aminoschutz­gruppe verwendet werden.

  在 D-、L-苯丙氨酸烷基酯或 L-苯丙氨酸烷基酯与 N-保护的 L-天冬氨酸的酶联过程中，可使用苯氧乙酰基、苯氧丙酰基或苯乙酰基作为氨基保护基团。
• Preparation of d-amino acids by enzymatic kinetic resolution using a mutant of penicillin-G acylase from E. coli
  作者：Chiara Carboni、Hans G.T. Kierkels、Lucia Gardossi、Kamil Tamiola、Dick B. Janssen、Peter J.L.M. Quaedflieg

  DOI：10.1016/j.tetasy.2005.12.023

  日期：2006.1

  We have demonstrated for the first time that D-glutamine (D-Gln) and D-glutamic acid (D-Glu) can be efficiently obtained in high ee (97% and 90%, respectively) by enzymatic kinetic resolution of D,L-Gln and D,L-Glu. This was achieved by enantioselective conversion of the L-enantiomers to their N-phenylacetyl derivatives in aqueous solution, using a mutant of penicillin-G acylase (PGA) from E coli and phenylacetic acid methylester as the acyl donor. Kinetic modeling studies suggest that the high ee values obtained are both due to a strong enantiopreference for the L-amino acid in the deacylation step of the covalent enzyme intermediate, as well as to completeness of conversion that is transiently obtained as a result of the distinct preference of the mutant PGA for phenylacetic acid methylester over the N-phenylacetyl-L-amino acid product. For the other amino acids tested (Asn, Asp, and Ser), the highest ee values that were obtained for the remaining D-enantiomer are moderate (50-80%)because of lower enantioselectivity in the enzyme deacylation step and due to less complete conversion of the L-amino acid caused by competition for the active site between the acyl donor and the N-phenylacetyl-L-amino acid that is produced. The results demonstrate that the mutated PGA has great potential for the production of optically active D-amino acids by kinetic resolution. (c) 2006 Published by Elsevier Ltd.
• SCHMIDT, KRWIN;KELLER, REINHOLD;SCHLINGMANN, MERTEN
  作者：SCHMIDT, KRWIN、KELLER, REINHOLD、SCHLINGMANN, MERTEN

  DOI：——

  日期：——