4-n-propanoyl-N-(cyclohexylcarbamoyl)benzenesulfonamide | 97021-37-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 4-n-propanoyl-N-(cyclohexylcarbamoyl)benzenesulfonamide
• 英文别名: N'-<4-Propionyl-benzolsulfonyl>-N-cyclohexyl-harnstoff；N-Cyclohexyl-N'-<4-propionyl-benzolsulfonyl>-harnstoff；1-Cyclohexyl-3-(4-propanoylphenyl)sulfonylurea
• CAS: 97021-37-9
• 化学式: C₁₆H₂₂N₂O₄S
• 分子量: 338.428
• InChiKey: YURCOAKGCRBXAP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  23
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-n-propanoylbenzenesulfonamide 、 环己基异氰酸酯 在 potassium carbonate 作用下， 以 丙酮 为溶剂， 反应 20.0h， 以72%的产率得到4-n-propanoyl-N-(cyclohexylcarbamoyl)benzenesulfonamide
  参考文献：
  名称：

  Catalytic Properties of Carbonyl Reductase from Rabbit Kidney for Acetohexamide and Its Analogs

  摘要：

  Analogs submitted by ethyl, n-propyl, n-butyl, and isopropyl groups instead of methyl group adjacent to a ketone group of acetohexamide were synthesized and the structural requirements of carbonyl reductase from rabbit kidney for these analogs were kinetically examined. The hydrophobicities in straight-chain alkyl groups of acetohexamide analogs were found to play an important role in the catalytic activity and substrate-binding capacity of the enzyme. We propose the possibility that a hydrophobic pocket is located in the substrate-binding domain of the enzyme. (C) 1998 Academic Press, Inc.

  DOI：

  10.1006/bioo.1994.1032

文献信息

• Catalytic Properties of Carbonyl Reductase from Rabbit Kidney for Acetohexamide and Its Analogs
  作者：Y. Imamura、T. Higuchi、M. Otagiri、S. Nagumo、H. Akita

  DOI：10.1006/bioo.1994.1032

  日期：1994.12

  Analogs submitted by ethyl, n-propyl, n-butyl, and isopropyl groups instead of methyl group adjacent to a ketone group of acetohexamide were synthesized and the structural requirements of carbonyl reductase from rabbit kidney for these analogs were kinetically examined. The hydrophobicities in straight-chain alkyl groups of acetohexamide analogs were found to play an important role in the catalytic activity and substrate-binding capacity of the enzyme. We propose the possibility that a hydrophobic pocket is located in the substrate-binding domain of the enzyme. (C) 1998 Academic Press, Inc.