N-乙酰基苯丙氨酰酪氨酰胺 | 19361-52-5

• 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: N-乙酰基苯丙氨酰酪氨酰胺
• 英文名称: Ac-Phe-Tyr-NH2
• 英文别名: N-Ac-Phe-Tyr-NH2；(2S)-2-acetamido-N-[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]-3-phenylpropanamide
• CAS: 19361-52-5
• 化学式: C₂₀H₂₃N₃O₄
• 分子量: 369.42
• InChiKey: NRNUHNDVXOFSJO-ROUUACIJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  27
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  122
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  N-乙酰-L-苯丙氨酸乙酯 、 L-酪氨酰胺 在 porcine pancreatic lipasetype II 作用下， 以 aq. buffer 为溶剂， 反应 0.06h， 以84.45%的产率得到N-乙酰基苯丙氨酰酪氨酰胺
  参考文献：
  名称：

  Formation of amide bond catalyzed by lipase in aqueous phase for peptide synthesis

  摘要：

  A dipeptide N-acetyl-L-phenylalanyl-L-tyrosinamide (N-Ac-Phe-Tyr-NH2), with angiotensin I converting enzyme (ACE) inhibitor activity, was synthesized via porcine pancreatic lipase catalyzed amidation of N-acetyl-phenylalanine ethyl ester with L-tyrosinamide in an aqueous phase. Response surface methodology was employed to evaluate the effects of synthesis parameters. The optimum synthesis conditions obtained an 84.45% yield of N-Ac-Phe-Tyr-NH2 with a reaction time of 3.8 min, a temperature of 20.9 degrees C, an enzyme amount of 6.5 U, and a substrate molar ratio of 2.5:1 (Tyr:Phe). The kinetics of lipase and alpha-chymotrypsin catalyzed amidation was compared using the Ping-Pong mechanism. The lipase showed a lower apparent kinetic constant than a-chymotrypsin indicating that the acyl lipase intermediate had a higher affinity toward tyrosinamide in the amidation. In addition, because the lipase can avoid the secondary hydrolysis of synthesized peptide, it is expected to be an effective method for obtaining a good yield of dipeptide. (C) 2016 Published by Elsevier B.V.

  DOI：

  10.1016/j.molcatb.2016.03.010