methyl 5-(N-(3-(3,4-dichlorobenzylthio)thiophene-2-carbonyl)sulfamoyl)-2-methoxybenzoate | 1336982-58-1

• 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: methyl 5-(N-(3-(3,4-dichlorobenzylthio)thiophene-2-carbonyl)sulfamoyl)-2-methoxybenzoate
• 英文别名: Methyl 5-[[3-[(3,4-dichlorophenyl)methylsulfanyl]thiophene-2-carbonyl]sulfamoyl]-2-methoxybenzoate
• CAS: 1336982-58-1
• 化学式: C₂₁H₁₇Cl₂NO₆S₃
• 分子量: 546.473
• InChiKey: IPLQJJXGYWHQSP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.4
• 重原子数：
  33
• 可旋转键数：
  9
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.14
• 拓扑面积：
  161
• 氢给体数：
  1
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  methyl 5-(N-(3-(3,4-dichlorobenzylthio)thiophene-2-carbonyl)sulfamoyl)-2-methoxybenzoate 在 水 、 lithium hydroxide 作用下， 以 甲醇 为溶剂， 以94%的产率得到5-(N-(3-(3,4-dichlorobenzylthio)thiophene-2-carbonyl)sulfamoyl)-2-methoxybenzoic acid
  参考文献：
  名称：

  Small Molecule Receptor Protein Tyrosine Phosphatase γ (RPTPγ) Ligands That Inhibit Phosphatase Activity via Perturbation of the Tryptophan–Proline–Aspartate (WPD) Loop

  摘要：

  Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of tyrosine residues, a process that involves a conserved tryptophan-proline-aspartate (WPD) loop in catalysis. In previously determined structures of PTPs, the WPD-loop has been observed in either an "open" conformation or a "closed" conformation. In the current work, X-ray structures of the catalytic domain of receptor-like protein tyrosine phosphatase gamma (RPTP gamma) revealed a ligand-induced "superopen" conformation not previously reported for PTPs. In the superopen conformation, the ligand acts as an apparent competitive inhibitor and binds in a small hydrophobic pocket adjacent to, but distinct from, the active site. In the open and closed WPD-loop conformations of RPTP gamma, the side chain of Trp1026 partially occupies this pocket. In the superopen conformation, Trp1026 is displaced allowing a 3,4-dichlorobenzyl substituent to occupy this site. The bound ligand prevents closure of the WPD-loop over the active site and disrupts the catalytic cycle of the enzyme.

  DOI：

  10.1021/jm2003766
• 作为产物：
  描述：

  3-ethoxythiocarbonylsulfanylthiophene-2-carboxylic acid methyl ester 在 4-二甲氨基吡啶 、 sodium methylate 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 sodium hydroxide 作用下， 以 甲醇 、 乙醇 、 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 14.0h， 生成 methyl 5-(N-(3-(3,4-dichlorobenzylthio)thiophene-2-carbonyl)sulfamoyl)-2-methoxybenzoate
  参考文献：
  名称：

  Small Molecule Receptor Protein Tyrosine Phosphatase γ (RPTPγ) Ligands That Inhibit Phosphatase Activity via Perturbation of the Tryptophan–Proline–Aspartate (WPD) Loop

  摘要：

  Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of tyrosine residues, a process that involves a conserved tryptophan-proline-aspartate (WPD) loop in catalysis. In previously determined structures of PTPs, the WPD-loop has been observed in either an "open" conformation or a "closed" conformation. In the current work, X-ray structures of the catalytic domain of receptor-like protein tyrosine phosphatase gamma (RPTP gamma) revealed a ligand-induced "superopen" conformation not previously reported for PTPs. In the superopen conformation, the ligand acts as an apparent competitive inhibitor and binds in a small hydrophobic pocket adjacent to, but distinct from, the active site. In the open and closed WPD-loop conformations of RPTP gamma, the side chain of Trp1026 partially occupies this pocket. In the superopen conformation, Trp1026 is displaced allowing a 3,4-dichlorobenzyl substituent to occupy this site. The bound ligand prevents closure of the WPD-loop over the active site and disrupts the catalytic cycle of the enzyme.

  DOI：

  10.1021/jm2003766