N-[(4-Ethoxy-phenylcarbamoyl)-methyl]-oxalamic acid | 141635-08-7

• 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-[(4-Ethoxy-phenylcarbamoyl)-methyl]-oxalamic acid
• 英文别名: 2-[[2-(4-Ethoxyanilino)-2-oxoethyl]amino]-2-oxoacetic acid
• CAS: 141635-08-7
• 化学式: C₁₂H₁₄N₂O₅
• 分子量: 266.254
• InChiKey: HONUJEXMXOTKTF-UHFFFAOYSA-N

物化性质

• 密度：
  1.354±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  19
• 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：
  105
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  N-[(4-Ethoxy-phenylcarbamoyl)-methyl]-oxalamic acid methyl ester 在 sodium hydroxide 作用下， 以 四氢呋喃 为溶剂， 反应 2.0h， 以85%的产率得到N-[(4-Ethoxy-phenylcarbamoyl)-methyl]-oxalamic acid
  参考文献：
  名称：

  Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analog N-oxaloglycine and its derivatives

  摘要：

  N-Oxaloglycine (3) is an alpha-ketoglutarate (1) analogue that is a competitive inhibitor of prolyl 4-hydroxylase (EC 1.14.11.2). A study of the structure-activity relationships of some other oxalo derivatives shows that substitution on the glycine moiety modulates activity stereoselectively and that if the omega-carboxylate is homologated or replaced by either acylsulfonamides or anilide, then activity is sharply reduced. This sensitivity to these changes is contrasted with the relative insensitivity of another putative alpha-ketoglutarate analogue, pyridine-2,5-dicarboxylic acid (2), and the implication is discussed that compounds of both series are unlikely to bind to prolyl hydroxylase in the same way even though both inhibit the enzyme competitively.

  DOI：

  10.1021/jm00092a016

文献信息

• Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analog N-oxaloglycine and its derivatives
  作者：C. Jane Cunliffe、Trevor J. Franklin、Neil J. Hales、George B. Hill

  DOI：10.1021/jm00092a016

  日期：1992.7

  N-Oxaloglycine (3) is an alpha-ketoglutarate (1) analogue that is a competitive inhibitor of prolyl 4-hydroxylase (EC 1.14.11.2). A study of the structure-activity relationships of some other oxalo derivatives shows that substitution on the glycine moiety modulates activity stereoselectively and that if the omega-carboxylate is homologated or replaced by either acylsulfonamides or anilide, then activity is sharply reduced. This sensitivity to these changes is contrasted with the relative insensitivity of another putative alpha-ketoglutarate analogue, pyridine-2,5-dicarboxylic acid (2), and the implication is discussed that compounds of both series are unlikely to bind to prolyl hydroxylase in the same way even though both inhibit the enzyme competitively.