[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl 3,4-diformylbenzoate | 752238-77-0

• 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: [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl 3,4-diformylbenzoate
• CAS: 752238-77-0
• 化学式: C₁₉H₁₇N₅O₇
• 分子量: 427.373
• InChiKey: KETYKOZCHKJRLB-SCFUHWHPSA-N

物化性质

• 沸点：
  821.9±75.0 °C(Predicted)
• 密度：
  1.74±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  31
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  180
• 氢给体数：
  3
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  C.I.酸性橙108 、 2-巯基乙醇 、 [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl 3,4-diformylbenzoate 以 水 、 乙腈 为溶剂， 反应 3.0h， 以32%的产率得到
  参考文献：
  名称：

  A Mechanism-Based Cross-Linker for the Identification of Kinase−Substrate Pairs

  摘要：

  The reversible phosphorylation of proteins is one of the most important mechanisms for the regulation of signal transduction cascades. Recently, there has been substantial progress made in the identification of new phosphoproteins and phosphorylation sites. Unfortunately, there are very few methods available that allow this information to be used to identify the upstream kinase responsible for the phosphorylation event. Herein, we describe a new method that allows the cross-linking of a substrate of interest to its upstream kinase. This method relies upon a novel, mechanism-based cross-linker and the replacement of the phosphorylated residue with a cysteine residue. The application of this method to a number of kinase-peptide substrate pairs is described.

  DOI：

  10.1021/ja048659i
• 作为产物：
  描述：

  ((3aR,4R,6R,6aR)-6-(6-amino-9H-purin-9-yl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methyl 1,3-dimethoxy-1,3-dihydroisobenzofuran-5-carboxylate 在 三氟乙酸 作用下， 反应 1.0h， 以42%的产率得到[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl 3,4-diformylbenzoate
  参考文献：
  名称：

  A Mechanism-Based Cross-Linker for the Identification of Kinase−Substrate Pairs

  摘要：

  The reversible phosphorylation of proteins is one of the most important mechanisms for the regulation of signal transduction cascades. Recently, there has been substantial progress made in the identification of new phosphoproteins and phosphorylation sites. Unfortunately, there are very few methods available that allow this information to be used to identify the upstream kinase responsible for the phosphorylation event. Herein, we describe a new method that allows the cross-linking of a substrate of interest to its upstream kinase. This method relies upon a novel, mechanism-based cross-linker and the replacement of the phosphorylated residue with a cysteine residue. The application of this method to a number of kinase-peptide substrate pairs is described.

  DOI：

  10.1021/ja048659i