| 440345-48-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 440345-48-2
• 化学式: C₄₉H₆₃N₃O₁₁Si
• 分子量: 898.138
• InChiKey: WUJPEIJUIZKKQD-PRZWQORUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.07
• 重原子数：
  64.0
• 可旋转键数：
  21.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.49
• 拓扑面积：
  158.13
• 氢给体数：
  0.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  在 48percent aq. tetrafluoroboric acid 作用下， 以 乙腈 为溶剂， 反应 0.08h， 以95%的产率得到methyl 2-azido-2-deoxy-3-O-benzyl-4-O-(2-O-acetyl-3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside
  参考文献：
  名称：

  α-(2,6)-Sialyltransferase-Catalyzed Sialylations of Conformationally Constrained Oligosaccharides

  摘要：

  It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galbeta(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver alpha-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficiencies.

  DOI：

  10.1021/ja0169771
• 作为产物：
  描述：

  methyl 2-azido-4,6-O-benzylidene-2-deoxy-β-D-glucopyranoside 在 咪唑 、 tetrafluoroboric acid 、 三氟化硼乙醚 、 sodium hydride 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 8.0h， 生成
  参考文献：
  名称：

  α-(2,6)-Sialyltransferase-Catalyzed Sialylations of Conformationally Constrained Oligosaccharides

  摘要：

  It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases. Correlation of the conformational properties of N-acetyl lactosamine (Galbeta(1-4)GlcNAc, LacNAc) and several preorganized derivatives with the corresponding apparent kinetic parameters of rat liver alpha-(2,6)-sialyltransferase-catalyzed sialylations revealed that this enzyme recognizes LacNAc in a low energy conformation. Furthermore, small variations in the conformational properties of the acceptors resulted in large differences in catalytic efficiency. Collectively, our data suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficiencies.

  DOI：

  10.1021/ja0169771