N--L-phenylalanine | 144085-32-5

• 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
• 英文名称: N--L-phenylalanine
• 英文别名: angiotensin I-converting enzyme；N-[N-(cyanoacetyl)-L-phenylalanyl]-L-phenylalanine；(2S)-2-[[(2S)-2-[(2-cyanoacetyl)amino]-3-phenylpropanoyl]amino]-3-phenylpropanoic acid
• CAS: 144085-32-5
• 化学式: C₂₁H₂₁N₃O₄
• 分子量: 379.415
• InChiKey: FPAPTZAOPMWDRV-ROUUACIJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  28
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  119
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  L-苯基丙氨酸叔丁酯 在 1-羟基苯并三唑一水物 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 14.5h， 生成 N--L-phenylalanine
  参考文献：
  名称：

  The first mechanism-based inactivators for angiotensin-converting enzyme

  摘要：

  The first example of mechanism-based inactivation of angiotensin-converting enzyme (ACE) is described for N-[N-(cyanoacetyl)-L-phenylalanyl]-L-phenylalanine (compound 1). It is proposed that an ACE-mediated deprotonation of 1 unmasks a ketenimine intermediate, which traps an active-site nucleophile, and hence irreversibly modifies the enzyme. In competition with the inactivation reaction, ACE also hydrolyzes 1 with a partition ratio of 8300 (i.e., k(cat)/k(inact)). Since the corresponding keto analogue, N-[(R)-2-benzyl-5-cyano-4-oxopentanoyl]-L-phenylalanine (compound 4), does not inactivate the enzyme, it is suggested that the NH in compound 1 is critical for the proper active-site anchoring of the inhibitor for the inactivation process to take place.

  DOI：

  10.1021/jm00100a024

文献信息

• The first mechanism-based inactivators for angiotensin-converting enzyme
  作者：Soumitra S. Ghosh、Odile Said-Nejad、Juliatiek Roestamadji、Shahriar Mobashery

  DOI：10.1021/jm00100a024

  日期：1992.10

  The first example of mechanism-based inactivation of angiotensin-converting enzyme (ACE) is described for N-[N-(cyanoacetyl)-L-phenylalanyl]-L-phenylalanine (compound 1). It is proposed that an ACE-mediated deprotonation of 1 unmasks a ketenimine intermediate, which traps an active-site nucleophile, and hence irreversibly modifies the enzyme. In competition with the inactivation reaction, ACE also hydrolyzes 1 with a partition ratio of 8300 (i.e., k(cat)/k(inact)). Since the corresponding keto analogue, N-[(R)-2-benzyl-5-cyano-4-oxopentanoyl]-L-phenylalanine (compound 4), does not inactivate the enzyme, it is suggested that the NH in compound 1 is critical for the proper active-site anchoring of the inhibitor for the inactivation process to take place.