N-acetyl-D-tryptophan ethyl ester | 92520-19-9

• 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-D-tryptophan ethyl ester
• 英文别名: N-acetyl-L-tryptophan ethyl ester；N^α-acetyl-D-tryptophan-ethyl ester；N^α-Acetyl-D-tryptophan-aethylester；ethyl (2R)-2-acetamido-3-(1H-indol-3-yl)propanoate
• CAS: 92520-19-9
• 化学式: C₁₅H₁₈N₂O₃
• 分子量: 274.32
• InChiKey: KQGQONPKSKUHHT-CQSZACIVSA-N

物化性质

• 沸点：
  517.6±40.0 °C(Predicted)
• 密度：
  1.208±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  20
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  71.2
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  乙醇 、 N-乙酰-D-色氨酸 在 native α-chymotrypsin imprinted with N-acetyl-D-tryptophan 作用下， 以 环己烷 为溶剂， 生成 N-acetyl-D-tryptophan ethyl ester
  参考文献：
  名称：

  Crosslinking of imprinted proteases to maintain a tailor-made substrate selectivity in aqueous solutions

  摘要：

  A covalent method to keep imprinted properties of proteins stable in aqueous as well as in organic environment is described. To stabilize the ligand induced acceptance for D-configured substrates by alpha-chymotrypsin or subtilisin Carlsberg, each protein was first vinylated by acylation with itaconic anhydride. Then, the tailoring of the derivatized proteins by precipitation in the presence of N-acetyl-D-tryptophan from an aqueous medium with l-propanol, and the subsequent crosslinking of the enzyme preparations with ethylene glycol dimethacrylate in cyclohexane was carried out. The crosslinked imprinted proteins (CLIPs) obtained catalyzed the hydrolysis of N-acetyl-D-tryptophan ethyl ester in phosphate buffer and the corresponding back reaction in cyclohexane, respectively. The repeated use of CLIP-alpha-chymotrypsin in D-ester hydrolysis was demonstrated. Furthermore, this particular CLIP-alpha-chymotrypsin showed no loss in activity when it subsequently was used in the synthesis of N-acetyl-D-tryptophan ethyl ester in cyclohexane again. In the case of D-ester hydrolysis the reaction rate acceleration (k(enz)/k(nonenz)) was in the same order of magnitude of about 10(4) -10(5) mM(-1) for the two CLIP-proteases. The results suggest that enzymes tailored by imprinting technique do not lose their induced "new" property in the presence of water when they are prepared according to the described vinylation/crosslinking method (CLIP technique). (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(99)00156-x

文献信息

• The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of Acetyl- and Nicotinyl-L-phenylalaninamide in Aqueous Solutions at 25° and pH 7.9¹
  作者：H. T. Huang、Robert J. Foster、Carl Niemann

  DOI：10.1021/ja01121a024

  日期：1952.1
• Resolution of N-protected amino acid esters using whole cells of Candida parapsilosis ATCC 7330
  作者：Selvaraj Stella、Anju Chadha

  DOI：10.1016/j.tetasy.2010.02.011

  日期：2010.3

  Whole cells of Candida parapsilosis ATCC 7330 were used for the resolution of N-acetyl amino acid esters. Excellent enantioselectivities (E = 40 to >500) were achieved for the resolution of N-protected protein and non-protein amino acid esters giving good yields (28-50%) and high enantiomeric excesses (up to >99%) for both enantiomers. (C) 2010 Elsevier Ltd. All rights reserved.
• Ståhl, Marianne; Jeppsson-Wistrand, Ulla; Månsson, Mats-Olle, Journal of the American Chemical Society, 1991, vol. 113, # 24, p. 9366 - 9368
  作者：Ståhl, Marianne、Jeppsson-Wistrand, Ulla、Månsson, Mats-Olle、Mosbach, Klaus

  DOI：——

  日期：——
• Crosslinking of imprinted proteases to maintain a tailor-made substrate selectivity in aqueous solutions
  作者：Fabian Peißker、Lutz Fischer

  DOI：10.1016/s0968-0896(99)00156-x

  日期：1999.10

  A covalent method to keep imprinted properties of proteins stable in aqueous as well as in organic environment is described. To stabilize the ligand induced acceptance for D-configured substrates by alpha-chymotrypsin or subtilisin Carlsberg, each protein was first vinylated by acylation with itaconic anhydride. Then, the tailoring of the derivatized proteins by precipitation in the presence of N-acetyl-D-tryptophan from an aqueous medium with l-propanol, and the subsequent crosslinking of the enzyme preparations with ethylene glycol dimethacrylate in cyclohexane was carried out. The crosslinked imprinted proteins (CLIPs) obtained catalyzed the hydrolysis of N-acetyl-D-tryptophan ethyl ester in phosphate buffer and the corresponding back reaction in cyclohexane, respectively. The repeated use of CLIP-alpha-chymotrypsin in D-ester hydrolysis was demonstrated. Furthermore, this particular CLIP-alpha-chymotrypsin showed no loss in activity when it subsequently was used in the synthesis of N-acetyl-D-tryptophan ethyl ester in cyclohexane again. In the case of D-ester hydrolysis the reaction rate acceleration (k(enz)/k(nonenz)) was in the same order of magnitude of about 10(4) -10(5) mM(-1) for the two CLIP-proteases. The results suggest that enzymes tailored by imprinting technique do not lose their induced "new" property in the presence of water when they are prepared according to the described vinylation/crosslinking method (CLIP technique). (C) 1999 Elsevier Science Ltd. All rights reserved.