(1S,3R)-1-(9-adenenyl)-3-(methyl-carboxymethoxy)-4-cyclopentene | 426225-84-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 咪唑并嘧啶类
• 英文名称: (1S,3R)-1-(9-adenenyl)-3-(methyl-carboxymethoxy)-4-cyclopentene
• 英文别名: methyl 2-[(1R,4S)-4-(6-aminopurin-9-yl)cyclopent-2-en-1-yl]oxyacetate
• CAS: 426225-84-5
• 化学式: C₁₃H₁₅N₅O₃
• 分子量: 289.294
• InChiKey: WQFQYOGCNJCLBE-BDAKNGLRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  21
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  105
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  (1S,3R)-1-(9-adenenyl)-3-(methyl-carboxymethoxy)-4-cyclopentene 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 为溶剂， 生成 (1R,3S)-1-(9-adenenyl)-3-(methyl-carboxymethoxy)cyclopentane
  参考文献：
  名称：

  Hydroxamate based inhibitors of adenylyl cyclase. Part 2: The effect of cyclic linkers on P-site binding

  摘要：

  The adenylyl cyclases (ACs) are a family of enzymes that are key elements of signal transduction by virtue of their ability to convert ATP to cAMP. The catalytic mechanism of this transformation proceeds through initial binding of ATP to the purine binding site (P-site) followed by metal mediated cyclization with loss of pyrophosphate. Previous work in our group identified novel inhibitors which possess an adenine ring joined to a metal-coordinating hydroxamic acid through flexible linkers. Considering the spatial positioning of the metals with respect to the adenine binding site coupled with potentially favorable entropic factors, conformational restriction of the tether through a stereochemistry based SAR employing a rigid cyclic scaffold was explored. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(02)00654-6
• 作为产物：
  描述：

  2-环戊烯-1-醇,4-[[(1,1-二甲基乙基)二甲基甲硅烷基]氧代]-,(1R,4S)- 在 dirhodium tetraacetate 、 sodium methylate 、 溶剂黄146 、 三苯基膦 、 偶氮二甲酸二乙酯 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 为溶剂， 生成 (1S,3R)-1-(9-adenenyl)-3-(methyl-carboxymethoxy)-4-cyclopentene
  参考文献：
  名称：

  Hydroxamate based inhibitors of adenylyl cyclase. Part 2: The effect of cyclic linkers on P-site binding

  摘要：

  The adenylyl cyclases (ACs) are a family of enzymes that are key elements of signal transduction by virtue of their ability to convert ATP to cAMP. The catalytic mechanism of this transformation proceeds through initial binding of ATP to the purine binding site (P-site) followed by metal mediated cyclization with loss of pyrophosphate. Previous work in our group identified novel inhibitors which possess an adenine ring joined to a metal-coordinating hydroxamic acid through flexible linkers. Considering the spatial positioning of the metals with respect to the adenine binding site coupled with potentially favorable entropic factors, conformational restriction of the tether through a stereochemistry based SAR employing a rigid cyclic scaffold was explored. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(02)00654-6