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 | 201594-43-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 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
• CAS: 201594-43-6
• 化学式: C₁₂H₁₇N₃O₅
• 分子量: 283.284
• InChiKey: AQHCMRFXUWRVIQ-UGKPPGOTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.12
• 重原子数：
  20.0
• 可旋转键数：
  2.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  116.84
• 氢给体数：
  4.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  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 在 sodium tetrahydroborate 作用下， 以 甲醇 、 水 为溶剂， 以76%的产率得到(2R,3S,4R,5R)-2-Hydroxymethyl-5-(8-hydroxy-5,6,7,8-tetrahydro-4H-1,3,4-triaza-azulen-3-yl)-tetrahydro-furan-3,4-diol
  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：

  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