α-D-NeuAc-(2->6)-β-D-Gal-(1->4)-β-D-GlcNAc-OCH3 | 100605-30-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: α-D-NeuAc-(2->6)-β-D-Gal-(1->4)-β-D-GlcNAc-OCH3
• 英文别名: NeuAcα2->6Galβ1->4GlcNAcβ-OMe；NeuAc(a2-6)Gal(b1-4)b-GlcNAc1Me；(2R,4S,5R,6R)-5-acetamido-2-[[(2R,3R,4S,5R,6S)-6-[(2R,3S,4R,5R,6R)-5-acetamido-4-hydroxy-2-(hydroxymethyl)-6-methoxyoxan-3-yl]oxy-3,4,5-trihydroxyoxan-2-yl]methoxy]-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid
• CAS: 100605-30-9
• 化学式: C₂₆H₄₄N₂O₁₉
• 分子量: 688.637
• InChiKey: GDDSOACCIHXJML-WBZWEQEOSA-N

物化性质

• 沸点：
  1146.9±65.0 °C(Predicted)
• 密度：
  1.63±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -7.2
• 重原子数：
  47
• 可旋转键数：
  13
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  333
• 氢给体数：
  12
• 氢受体数：
  19

反应信息

• 作为产物：
  描述：

  cytidine-5'-monophosphono-N-acetylneuraminic acid 、 N-acetyllactosamine methyl glycoside 在 bovine serum albumin 、 Triton 100 α-(2,6)-sialyltransferase 、 sodium cacodylate buffer 、 alkaline phosphatase 作用下， 反应 36.0h， 生成 α-D-NeuAc-(2->6)-β-D-Gal-(1->4)-β-D-GlcNAc-OCH3
  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

文献信息

• α-(2,6)-Sialyltransferase-Catalyzed Sialylations of Conformationally Constrained Oligosaccharides
  作者：M. Carmen Galan、Andre P. Venot、John Glushka、Anne Imberty、Geert-Jan Boons

  DOI：10.1021/ja0169771

  日期：2002.5.1

  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.