3-carboxylphenyl 1-benzyl-2-oxo-pyrrolidine-3-carboxylate | 1208236-22-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚酯
• 英文名称: 3-carboxylphenyl 1-benzyl-2-oxo-pyrrolidine-3-carboxylate
• 英文别名: 3-(1-Benzyl-2-oxopyrrolidine-3-carbonyl)oxybenzoic acid
• CAS: 1208236-22-9
• 化学式: C₁₉H₁₇NO₅
• 分子量: 339.348
• InChiKey: NDWRWCHFQVKWRB-UHFFFAOYSA-N

物化性质

• 沸点：
  599.5±50.0 °C(Predicted)
• 密度：
  1.356±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  25
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  83.9
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  3-carboxylphenyl 1-benzyl-2-oxo-pyrrolidine-3-carboxylate 在 水 、 Enterobacter cloacae P99 β-lactamase 作用下， 以 二甲基亚砜 为溶剂， 生成 间羟基苯甲酸
  参考文献：
  名称：

  Substituted aryl malonamates as new serine β-lactamase substrates: Structure–activity studies

  摘要：

  A series of substituted aryl malonamates have been prepared. These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced by a retro-amide. Like the phenaceturates, these compounds are substrates of typical class A and class C beta-lactamases, particularly of the latter, and of soluble DD-peptidases. The effect of substituents alpha to the ester carbonyl group on turnover by these enzymes is similar to that in the phenaceturates. On the other hand, N-alkylation of the side chain amide of malonamates, but not of phenaceturates, retains the susceptibility of the compounds to hydrolysis by beta-lactamases. This reactivity is not enhanced, however, by bridging the amide nitrogen and C alpha atoms. A phosphonate analogue of the malonamates was found to be an irreversible inhibitor of the beta-lactamases. These results, therefore, provide further evidence for the covalent access of compounds bearing retroamide side chains to the active sites of beta-lactam-recognizing enzymes. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.10.056
• 作为产物：
  描述：

  3-benzyloxycarbonylphenyl 1-benzyl-2-oxo-pyrrolidine-3-carboxylate 在 palladium 10% on activated carbon 、 氢气 作用下， 以 乙酸乙酯 为溶剂， 反应 2.0h， 生成 3-carboxylphenyl 1-benzyl-2-oxo-pyrrolidine-3-carboxylate
  参考文献：
  名称：

  Substituted aryl malonamates as new serine β-lactamase substrates: Structure–activity studies

  摘要：

  A series of substituted aryl malonamates have been prepared. These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced by a retro-amide. Like the phenaceturates, these compounds are substrates of typical class A and class C beta-lactamases, particularly of the latter, and of soluble DD-peptidases. The effect of substituents alpha to the ester carbonyl group on turnover by these enzymes is similar to that in the phenaceturates. On the other hand, N-alkylation of the side chain amide of malonamates, but not of phenaceturates, retains the susceptibility of the compounds to hydrolysis by beta-lactamases. This reactivity is not enhanced, however, by bridging the amide nitrogen and C alpha atoms. A phosphonate analogue of the malonamates was found to be an irreversible inhibitor of the beta-lactamases. These results, therefore, provide further evidence for the covalent access of compounds bearing retroamide side chains to the active sites of beta-lactam-recognizing enzymes. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.10.056

文献信息

• Substituted aryl malonamates as new serine β-lactamase substrates: Structure–activity studies
  作者：S.A. Adediran、D. Cabaret、J.-F. Lohier、M. Wakselman、R.F. Pratt

  DOI：10.1016/j.bmc.2009.10.056

  日期：2010.1

  A series of substituted aryl malonamates have been prepared. These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced by a retro-amide. Like the phenaceturates, these compounds are substrates of typical class A and class C beta-lactamases, particularly of the latter, and of soluble DD-peptidases. The effect of substituents alpha to the ester carbonyl group on turnover by these enzymes is similar to that in the phenaceturates. On the other hand, N-alkylation of the side chain amide of malonamates, but not of phenaceturates, retains the susceptibility of the compounds to hydrolysis by beta-lactamases. This reactivity is not enhanced, however, by bridging the amide nitrogen and C alpha atoms. A phosphonate analogue of the malonamates was found to be an irreversible inhibitor of the beta-lactamases. These results, therefore, provide further evidence for the covalent access of compounds bearing retroamide side chains to the active sites of beta-lactam-recognizing enzymes. (C) 2009 Elsevier Ltd. All rights reserved.