1-(1-Benzyl-5-nitro-1H-imidazol-4-yl)-4,4-dimethoxy-2-nitro-butan-1-one | 201594-38-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 1-(1-Benzyl-5-nitro-1H-imidazol-4-yl)-4,4-dimethoxy-2-nitro-butan-1-one
• CAS: 201594-38-9
• 化学式: C₁₆H₁₈N₄O₇
• 分子量: 378.342
• InChiKey: QXCHGADPMHSYCF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.68
• 重原子数：
  27.0
• 可旋转键数：
  10.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  139.63
• 氢给体数：
  0.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  1-(1-Benzyl-5-nitro-1H-imidazol-4-yl)-4,4-dimethoxy-2-nitro-butan-1-one 在 palladium dihydroxide 、 palladium on activated charcoal 氢气 、 sodium methylate 、 三氟乙酸 作用下， 以 甲醇 、 二氯甲烷 、 二氧化碳 、 水 、 溶剂黄146 为溶剂， 生成 3-((2R,3R,4S,5R)-3,4-Dihydroxy-5-hydroxymethyl-tetrahydro-furan-2-yl)-4,5,6,7-tetrahydro-3H-1,3,4-triaza-azulen-8-one
  参考文献：
  名称：

  Irreversible, Tight-Binding Inhibition of Adenosine Deaminase by Coformycins: Inhibitor Structural Features That Contribute to the Mode of Enzyme Inhibition

  摘要：

  Coformycin analogues 1-6 were synthesized and biochemically screened against adenosine deaminase in order to assess the relative contributions of N-4, N-6, and the N-3 sugar moiety to the mane of enzyme inhibition. Our results indicate that N-4 plays a relatively greater role than N-6 in enzyme tight-binding, and that a benzyl group can substitute for the sugar moiety at N-3. The absence of a sugar or benzyl group at N-3, however, leads to lass of activity. The hydroxyl group at C-8, while crucial for activity, does not alone confer the tight-binding characteristics to coformycins.

  DOI：

  10.1080/07328319708006131
• 作为产物：
  描述：

  5-硝基-1-(苯基甲基)-1H-咪唑-4-羧酸 在 potassium tert-butylate 作用下， 以 四氢呋喃 为溶剂， 生成 1-(1-Benzyl-5-nitro-1H-imidazol-4-yl)-4,4-dimethoxy-2-nitro-butan-1-one
  参考文献：
  名称：

  Irreversible, Tight-Binding Inhibition of Adenosine Deaminase by Coformycins: Inhibitor Structural Features That Contribute to the Mode of Enzyme Inhibition

  摘要：

  Coformycin analogues 1-6 were synthesized and biochemically screened against adenosine deaminase in order to assess the relative contributions of N-4, N-6, and the N-3 sugar moiety to the mane of enzyme inhibition. Our results indicate that N-4 plays a relatively greater role than N-6 in enzyme tight-binding, and that a benzyl group can substitute for the sugar moiety at N-3. The absence of a sugar or benzyl group at N-3, however, leads to lass of activity. The hydroxyl group at C-8, while crucial for activity, does not alone confer the tight-binding characteristics to coformycins.

  DOI：

  10.1080/07328319708006131