methyl 3-(4-(N-(3-chlorophenyl)-N-methylsulfamoyl)-2-nitrophenyl)-2-oxopropanoate | 1303575-50-9

• 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 3-(4-(N-(3-chlorophenyl)-N-methylsulfamoyl)-2-nitrophenyl)-2-oxopropanoate
• CAS: 1303575-50-9
• 化学式: C₁₇H₁₅ClN₂O₇S
• 分子量: 426.834
• InChiKey: CQTWMPYPTANOGE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.36
• 重原子数：
  28.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  123.89
• 氢给体数：
  0.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  methyl 3-(4-(N-(3-chlorophenyl)-N-methylsulfamoyl)-2-nitrophenyl)-2-oxopropanoate 在 tin(II) chloride dihdyrate 、 苯硫酚 、 三乙胺 作用下， 以 乙腈 为溶剂， 反应 0.08h， 生成 methyl 6-(N-(3-chlorophenyl)-N-methylsulfamoyl)-1-hydroxy-1H-indole-2-carboxylate
  参考文献：
  名称：

  Synthesis of sulfonamide-containing N-hydroxyindole-2-carboxylates as inhibitors of human lactate dehydrogenase-isoform 5

  摘要：

  N-Hydroxyindole-2-carboxylates possessing sulfonamide-substituents at either position 5 or 6 were designed and synthesized. The inhibitory activities of these compounds against isoforms 1 and 5 of human lactate dehydrogenase were analysed, and K-i values of the most efficient inhibitors were determined by standard enzyme kinetic studies. Some of these compounds displayed state-of-the-art inhibitory potencies against isoform 5 (K-i values as low as 5.6 mu M) and behaved as competitive inhibitors versus both the substrate and the cofactor. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.10.031
• 作为产物：
  描述：

  3-氯-N-甲基苯胺 在 sodium hydride 、 碳酸氢钠 作用下， 以 N,N-二甲基甲酰胺 、 mineral oil 为溶剂， 反应 0.5h， 生成 methyl 3-(4-(N-(3-chlorophenyl)-N-methylsulfamoyl)-2-nitrophenyl)-2-oxopropanoate
  参考文献：
  名称：

  Synthesis of sulfonamide-containing N-hydroxyindole-2-carboxylates as inhibitors of human lactate dehydrogenase-isoform 5

  摘要：

  N-Hydroxyindole-2-carboxylates possessing sulfonamide-substituents at either position 5 or 6 were designed and synthesized. The inhibitory activities of these compounds against isoforms 1 and 5 of human lactate dehydrogenase were analysed, and K-i values of the most efficient inhibitors were determined by standard enzyme kinetic studies. Some of these compounds displayed state-of-the-art inhibitory potencies against isoform 5 (K-i values as low as 5.6 mu M) and behaved as competitive inhibitors versus both the substrate and the cofactor. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.10.031