Xanthosine, 2-S-[(4-nitrophenyl)methyl]-2-thio- | 88868-74-0

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷
• 英文名称: Xanthosine, 2-S-[(4-nitrophenyl)methyl]-2-thio-
• 英文别名: 9-((2R,3R,4S,5R)-3,4-Dihydroxy-5-hydroxymethyl-tetrahydro-furan-2-yl)-2-(4-nitro-benzylsulfanyl)-1,9-dihydro-purin-6-one
• CAS: 88868-74-0
• 化学式: C₁₇H₁₇N₅O₇S
• 分子量: 435.417
• InChiKey: UXRKHPJWCKDEJF-XNIJJKJLSA-N

物化性质

• 密度：
  1.87±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.07
• 重原子数：
  30.0
• 可旋转键数：
  6.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  176.63
• 氢给体数：
  4.0
• 氢受体数：
  11.0

反应信息

• 作为反应物：
  描述：

  Xanthosine, 2-S-[(4-nitrophenyl)methyl]-2-thio- 在 磷酸三甲酯 、 三氯氧磷 作用下， 反应 5.0h， 以14%的产率得到Phosphoric acid mono-{(2R,3S,4R,5R)-3,4-dihydroxy-5-[2-(4-nitro-benzylsulfanyl)-6-oxo-1,6-dihydro-purin-9-yl]-tetrahydro-furan-2-ylmethyl} ester; compound with ammonia
  参考文献：
  名称：

  Inhibitors of inosinic acid dehydrogenase. 2-Substituted inosinic acids

  摘要：

  A series of 2-substituted inosine monophosphate (IMP) and inosine derivatives were synthesized and tested for inhibitory activity against IMP dehydrogenase from Escherichia coli. All of the IMP analogues that possessed electron-withdrawing substituents on the phenyl ring of a benzylthio group placed at the 2-position of IMP showed strong inhibition, which was competitive with IMP. No evidence of hydrophobic interactions of the 2-substituent with the enzyme was observed.

  DOI：

  10.1021/jm00370a003
• 作为产物：
  描述：

  2-Mercaptoinosin 、 alkaline earth salt of/the/ methylsulfuric acid 在 potassium carbonate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 以92%的产率得到Xanthosine, 2-S-[(4-nitrophenyl)methyl]-2-thio-
  参考文献：
  名称：

  Inhibitors of inosinic acid dehydrogenase. 2-Substituted inosinic acids

  摘要：

  A series of 2-substituted inosine monophosphate (IMP) and inosine derivatives were synthesized and tested for inhibitory activity against IMP dehydrogenase from Escherichia coli. All of the IMP analogues that possessed electron-withdrawing substituents on the phenyl ring of a benzylthio group placed at the 2-position of IMP showed strong inhibition, which was competitive with IMP. No evidence of hydrophobic interactions of the 2-substituent with the enzyme was observed.

  DOI：

  10.1021/jm00370a003