8-Hydroxy-4,6,7,8-tetrahydro-3H-imidazo[4,5-d][1,3]diazepin-5-one | 193904-37-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 咪唑二氮卓类
• 英文名称: 8-Hydroxy-4,6,7,8-tetrahydro-3H-imidazo[4,5-d][1,3]diazepin-5-one
• 英文别名: 8-hydroxy-4,6,7,8-tetrahydro-1H-imidazo[4,5-d][1,3]diazepin-5-one
• CAS: 193904-37-9
• 化学式: C₆H₈N₄O₂
• 分子量: 168.155
• InChiKey: FAYDIVOFOOYLHE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.6
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  90
• 氢给体数：
  4
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  8-Hydroxy-4,6,7,8-tetrahydro-3H-imidazo[4,5-d][1,3]diazepin-5-one 在 sodium methylate 作用下， 以 甲醇 为溶剂， 生成 3-((2R,3R,4S,5R)-3,4-Dihydroxy-5-hydroxymethyl-tetrahydro-furan-2-yl)-8-hydroxy-4,6,7,8-tetrahydro-3H-imidazo[4,5-d][1,3]diazepin-5-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：

  3-benzyl-4,5,6,7-tetrahydro-8H-imidazo[4,5-d][1,3]diazepine-5,8-dione 在 palladium dihydroxide sodium tetrahydroborate 、 氢气 作用下， 以 甲醇 、 水 、 溶剂黄146 为溶剂， 生成 8-Hydroxy-4,6,7,8-tetrahydro-3H-imidazo[4,5-d][1,3]diazepin-5-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

文献信息

• Irreversible, Tight-Binding Inhibition of Adenosine Deaminase by Coformycins: Inhibitor Structural Features That Contribute to the Mode of Enzyme Inhibition
  作者：Mikyung Hong、Ramachandra S. Hosmane

  DOI：10.1080/07328319708006131

  日期：1997.7

  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.