N-carboxymethoxy-4-toluenesulfonamide | 14962-35-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-carboxymethoxy-4-toluenesulfonamide
• 英文别名: 2-[(4-Methylphenyl)sulfonylamino]oxyacetic acid
• CAS: 14962-35-7
• 化学式: C₉H₁₁NO₅S
• mdl: MFCD19595964
• 分子量: 245.256
• InChiKey: VURKBJZBNVMFBO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.222
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  对甲苯磺酰氯 、 2-(氨基氧基)乙酸 在 potassium carbonate 作用下， 以 四氢呋喃 、 水 为溶剂， 反应 5.0h， 生成 N-carboxymethoxy-4-toluenesulfonamide
  参考文献：
  名称：

  Carbonic anhydrase inhibitors. Part 37. Novel classes of isozyme I and II inhibitors and their mechanism of action. Kinetic and spectroscopic investigations on native and cobalt-substituted enzymes

  摘要：

  The interaction of Zn(II)- and Co(II)-carbonic anhydrase (CA) with a series of compounds possessing moieties resembling the aromatic sulfonamides, such as sulfamide, sulfamic acid, N-substituted aromatic sulfonamides, sulfenamides, sulfinic and seleninic acids, was investigated using kinetic and spectroscopic techniques. All these compounds inhibit the hydrasic and esterasic activity of the enzyme. Their binding within the active site of isozymes I and IT is discussed on the basis of modifications of electronic and IH-NMR spectra of their adducts with the Co(II) enzyme. Some of these compounds represent novel classes of CA inhibitors, possessing equal or stronger potencies than the prototypical inhibitors, the unsubstituted sulfonamides. Qualitative structure-activity correlations are discussed.

  DOI：

  10.1016/s0223-5234(97)86179-x

文献信息

• Carbonic anhydrase inhibitors. Part 37. Novel classes of isozyme I and II inhibitors and their mechanism of action. Kinetic and spectroscopic investigations on native and cobalt-substituted enzymes
  作者：F Briganti、R Pierattelli、A Scozzafava、CT Supuran

  DOI：10.1016/s0223-5234(97)86179-x

  日期：1996.1

  The interaction of Zn(II)- and Co(II)-carbonic anhydrase (CA) with a series of compounds possessing moieties resembling the aromatic sulfonamides, such as sulfamide, sulfamic acid, N-substituted aromatic sulfonamides, sulfenamides, sulfinic and seleninic acids, was investigated using kinetic and spectroscopic techniques. All these compounds inhibit the hydrasic and esterasic activity of the enzyme. Their binding within the active site of isozymes I and IT is discussed on the basis of modifications of electronic and IH-NMR spectra of their adducts with the Co(II) enzyme. Some of these compounds represent novel classes of CA inhibitors, possessing equal or stronger potencies than the prototypical inhibitors, the unsubstituted sulfonamides. Qualitative structure-activity correlations are discussed.