2-amino-4-diethylsulfamoyl-butyric acid | 90203-54-6

• 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: 2-amino-4-diethylsulfamoyl-butyric acid
• 英文别名: 2-Amino-4-diaethylsulfamoyl-buttersaeure；2-Amino-4-(diethylsulfamoyl)butanoic acid
• CAS: 90203-54-6
• 化学式: C₈H₁₈N₂O₄S
• 分子量: 238.308
• InChiKey: DOELBOGKIYJUDB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 重原子数：
  15
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  109
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  (+/-)-5-<2-(N,N-Diaethyl-sulfamoyl)-aethyl>-hydantoin 在 barium dihydroxide 作用下， 生成 2-amino-4-diethylsulfamoyl-butyric acid
  参考文献：
  名称：

  Potential Anticancer Agents.¹ VI. Synthesis of α-Amino-γ-sulfamoylbutyric Acids with Substituents on the Sulfonamide Nitrogen

  摘要：

  DOI：

  10.1021/jo01103a005

文献信息

• Investigation of Mechanism of Nitrogen Transfer in Glucosamine 6-Phosphate Synthase with the Use of Transition State Analogs
  作者：Sławomir Milewski、Maria Hoffmann、Ryszard Andruszkiewicz、Edward Borowski

  DOI：10.1006/bioo.1997.1077

  日期：1997.10

  Several structural analogs of putative tetrahedral intermediates of the reaction catalysed by the glutamine amide transfer domain of Candida albicans glucosamine 6-phosphate synthase have been designed and synthesized. Esters and amides of gamma-phosphonic and gamma-sulfonic analogs of glutamine and glutamic acid were tested as potential inhibitors of the enzyme. N-substituted amides 9 and 15 were found to be the strongest inhibitors in the series. Structure-activity relationship studies led to conclusions supporting the possibility of a direct nucleophilic attack of the glutamine amide nitrogen on an electrophilic site of the enzyme-bound fructose 6-phosphate as the most likely mechanism of nitrogen transfer in glucosamine 6-phosphate synthase. (C) 1997 Academic Press.
• Potential Anticancer Agents.¹ VI. Synthesis of α-Amino-γ-sulfamoylbutyric Acids with Substituents on the Sulfonamide Nitrogen
  作者：CAROL W. MOSHER、R. M. SILVERSTEIN、OSBORNE P. CREWS、B. R. BAKER

  DOI：10.1021/jo01103a005

  日期：1958.9