3-benzoylpropionylglycine | 75162-15-1

• 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: 3-benzoylpropionylglycine
• 英文别名: N-(3-benzoylpropanoyl)glycine；N-(3-benzoylpropionyl)-L-glycine；N-(4-Oxo-4-phenylbutanoyl)glycine；2-[(4-oxo-4-phenylbutanoyl)amino]acetic acid
• CAS: 75162-15-1
• 化学式: C₁₂H₁₃NO₄
• 分子量: 235.24
• InChiKey: OFGZDNHLYGPHIU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  17
• 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：
  83.5
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-benzoylpropionylglycine 生成 N-(3-benzoylpropanoyl)glycyl-L-phenylalanine
  参考文献：
  名称：

  Effect of Enzyme–Substrate Interactions Away from the Reaction Site on Carboxypeptidase A Catalysis

  摘要：

  The kinetics of 14 peptide substrates of carboxypeptidase A have been studied for the purpose of evaluating P-1-P-3/S-1-S-3 interactions. It was found that the amide group at P-1-P-2 is required for efficient catalysis. This observation is consistent with previously proposed hydrogen bonding interactions, based on crystallographic data, between the P-1 NH and Tyr-248 and between the P-2 carbonyl oxygen and Arg-71. In contrast, substitution of the benzamido amide group (at P-2-P-3) Of N-benzoylglycylglycyl-1-phenylalanine by -CH2CH2- resulted in more effective catalysis. In this case hydrophobic interactions are important in the ground state and in the transition state of the rate-determining step. (C) 1996 Academic Press. Inc.

  DOI：

  10.1006/bioo.1996.0026
• 作为产物：
  描述：

  N-(1,4-二氧代-4-苯基丁基)甘氨酸甲酯 以65.1%的产率得到3-benzoylpropionylglycine
  参考文献：
  名称：

  Effect of Enzyme–Substrate Interactions Away from the Reaction Site on Carboxypeptidase A Catalysis

  摘要：

  The kinetics of 14 peptide substrates of carboxypeptidase A have been studied for the purpose of evaluating P-1-P-3/S-1-S-3 interactions. It was found that the amide group at P-1-P-2 is required for efficient catalysis. This observation is consistent with previously proposed hydrogen bonding interactions, based on crystallographic data, between the P-1 NH and Tyr-248 and between the P-2 carbonyl oxygen and Arg-71. In contrast, substitution of the benzamido amide group (at P-2-P-3) Of N-benzoylglycylglycyl-1-phenylalanine by -CH2CH2- resulted in more effective catalysis. In this case hydrophobic interactions are important in the ground state and in the transition state of the rate-determining step. (C) 1996 Academic Press. Inc.

  DOI：

  10.1006/bioo.1996.0026

文献信息

• Rivett, Donald E.; Stewart, Frederick H. C., Australian Journal of Chemistry, 1980, vol. 33, # 3, p. 625 - 631
  作者：Rivett, Donald E.、Stewart, Frederick H. C.

  DOI：——

  日期：——
• MCEVOY, F. J.;ALBRIGHT, J. D.
  作者：MCEVOY, F. J.、ALBRIGHT, J. D.

  DOI：——

  日期：——
• US4435329A
  申请人：——

  公开号：US4435329A

  公开（公告）日：1984-03-06
• Effect of Enzyme–Substrate Interactions Away from the Reaction Site on Carboxypeptidase A Catalysis
  作者：John F. Sebastian、Guiqing Liang、Annissa Jabarin、Karen Thomas、H.Bonnie Wu

  DOI：10.1006/bioo.1996.0026

  日期：1996.9

  The kinetics of 14 peptide substrates of carboxypeptidase A have been studied for the purpose of evaluating P-1-P-3/S-1-S-3 interactions. It was found that the amide group at P-1-P-2 is required for efficient catalysis. This observation is consistent with previously proposed hydrogen bonding interactions, based on crystallographic data, between the P-1 NH and Tyr-248 and between the P-2 carbonyl oxygen and Arg-71. In contrast, substitution of the benzamido amide group (at P-2-P-3) Of N-benzoylglycylglycyl-1-phenylalanine by -CH2CH2- resulted in more effective catalysis. In this case hydrophobic interactions are important in the ground state and in the transition state of the rate-determining step. (C) 1996 Academic Press. Inc.