N-benzyl-2-methoxymalonamic acid methyl ester | 1208236-27-4

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: N-benzyl-2-methoxymalonamic acid methyl ester
• 英文别名: Methyl 3-(benzylamino)-2-methoxy-3-oxopropanoate
• CAS: 1208236-27-4
• 化学式: C₁₂H₁₅NO₄
• 分子量: 237.255
• InChiKey: NLIKDHPAWNHZCJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  17
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  64.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-benzyl-2-methoxymalonamic acid methyl ester 在 水 、 sodium hydroxide 作用下， 以 甲醇 、 水 为溶剂， 以86%的产率得到N-benzyl-2-methoxymalonamic acid
  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 These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced by a retro-amide.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：

  苄胺 、 3-氯-2-甲氧基-3-氧代丙酸甲酯 以 二氯甲烷 为溶剂， 反应 1.0h， 以67%的产率得到N-benzyl-2-methoxymalonamic acid methyl ester
  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 These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced by a retro-amide.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