N-(benzyloxy)-6--N'-(tert-butoxycarbonyl)amino>hexanamide | 142160-54-1

• 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: N-(benzyloxy)-6--N'-(tert-butoxycarbonyl)amino>hexanamide
• 英文别名: N-(benzyloxy)-6--N'-(tert-butoxycarbonyl)amino>hexanamide
• CAS: 142160-54-1
• 化学式: C₂₆H₄₃N₃O₆
• 分子量: 493.644
• InChiKey: FYDREQSXJGFGRM-UHFFFAOYSA-N

物化性质

• 密度：
  1.085±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.95
• 重原子数：
  35.0
• 可旋转键数：
  13.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  106.2
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  N-(benzyloxy)-6--N'-(tert-butoxycarbonyl)amino>hexanamide 在 盐酸 作用下， 反应 1.0h， 以0.5 g的产率得到N⁸-acetylspermidine
  参考文献：
  名称：

  Inhibition of N8-acetylspermidine deacetylase by active-site-directed metal coordinating inhibitors

  摘要：

  A number of substrate analogues of N8-acetylspermidine (N8-AcSpd) (16) and chemical modifying agents containing metal coordinating ligands were assayed as inhibitors of the cytoplasmic enzyme N8-AcSpd deacetylase from rat liver. The enzyme is inhibited by metal chelators, several omega-amino-substituted carboxylic acids, and some thiol reagents. Inhibition by diisopropyl fluorophosphate was observed only at high concentrations. These results suggest that the catalytic mechanism of the enzyme requires a transition state metal and free sulfhydryl groups for activity. The most potent inhibitor synthesized 6-[(3-aminopropyl)amino]-N-hydroxyhexanamide (15), has an apparent K(i) of 0.001-mu-M. It binds to the target enzyme 11 000 times tighter than the substrate (apparent K(m) = 11-mu-M). These compounds and a previously reported series of compounds (Dredar, S. A.; Blankenship, J. W.; Marchant, P. E.; Manneh, V. A.; Fries, D. S. J. Med. Chem. 1989, 32, 984-989) are useful in mapping the active site and determining the physiological function of N8-AcSpd deacetylase.

  DOI：

  10.1021/jm00091a009
• 作为产物：
  描述：

  ethyl 6-<<<3-(tert-butoxycarbonyl)amino>propyl>amino>hexanoate 在 sodium hydroxide 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 乙醇 、 氯仿 为溶剂， 反应 102.0h， 生成 N-(benzyloxy)-6--N'-(tert-butoxycarbonyl)amino>hexanamide
  参考文献：
  名称：

  Inhibition of N8-acetylspermidine deacetylase by active-site-directed metal coordinating inhibitors

  摘要：

  A number of substrate analogues of N8-acetylspermidine (N8-AcSpd) (16) and chemical modifying agents containing metal coordinating ligands were assayed as inhibitors of the cytoplasmic enzyme N8-AcSpd deacetylase from rat liver. The enzyme is inhibited by metal chelators, several omega-amino-substituted carboxylic acids, and some thiol reagents. Inhibition by diisopropyl fluorophosphate was observed only at high concentrations. These results suggest that the catalytic mechanism of the enzyme requires a transition state metal and free sulfhydryl groups for activity. The most potent inhibitor synthesized 6-[(3-aminopropyl)amino]-N-hydroxyhexanamide (15), has an apparent K(i) of 0.001-mu-M. It binds to the target enzyme 11 000 times tighter than the substrate (apparent K(m) = 11-mu-M). These compounds and a previously reported series of compounds (Dredar, S. A.; Blankenship, J. W.; Marchant, P. E.; Manneh, V. A.; Fries, D. S. J. Med. Chem. 1989, 32, 984-989) are useful in mapping the active site and determining the physiological function of N8-AcSpd deacetylase.

  DOI：

  10.1021/jm00091a009