NeuAc(a2-3)[NeuAc(a2-6)]Gal(b1-4)Glc

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: NeuAc(a2-3)[NeuAc(a2-6)]Gal(b1-4)Glc
• 英文别名: (2R,4S,5R,6R)-5-acetamido-2-[[(2R,3S,4S,5R,6S)-4-[(2S,4S,5R,6R)-5-acetamido-2-carboxy-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxan-2-yl]oxy-3,5-dihydroxy-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-2-yl]methoxy]-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid
• 化学式: C₃₄H₅₆N₂O₂₇
• 分子量: 924.816
• InChiKey: UNBPDLSRKXGUBJ-DVDGJGEMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -10.2
• 重原子数：
  63
• 可旋转键数：
  18
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  481
• 氢给体数：
  18
• 氢受体数：
  27

反应信息

• 作为产物：
  描述：

  N-乙酰神经氨酸水合物 、 3'-sialyllactose 在 苯磺酰胺 、 alkalinephosphatase 、 sialyltransferase 作用下， 反应 2.0h， 以92%的产率得到NeuAc(a2-3)[NeuAc(a2-6)]Gal(b1-4)Glc
  参考文献：
  名称：

  A Novel α-2,6-Sialyltransferase:  Transfer of Sialic Acid to Fucosyl and Sialyl Trisaccharides

  摘要：

  The substrate specificity and enzymatic sialylation ability of the bacterium alpha-2,6-sialyltransferase were examined. The enzyme assay displayed a remarkable ability to catalyze sialyl transfer to type-II oligosaccharides possessing fucoside or sialoside at the 2 or 3 position of the terminal galactoside. Enzymatic syntheses were performed in order to confirm the structure of unusual assay products found when using Neu5Ac beta 2,3Gal beta 1,4Glc and Fuc alpha 1,2Gal beta 1,4Glc as the sialyl accepters. Both sialylation reactions (10 mu mol scales) were run using 83 munits of enzyme, were complete in 2 h, and afforded the sialoside analogues Neu5Ac alpha 2,6(Fuc alpha 1,2) Gal beta 1,4Glc (88%) and Neu5Ac alpha 2,6(Neu5Ac beta 2,3) Gal beta 1,4Glc (92%).

  DOI：

  10.1021/jo961214v

文献信息

• A Novel α-2,6-Sialyltransferase:  Transfer of Sialic Acid to Fucosyl and Sialyl Trisaccharides
  作者：Yasuhiro Kajihara、Takeshi Yamamoto、Hideki Nagae、Motoko Nakashizuka、Tohru Sakakibara、Ichiro Terada

  DOI：10.1021/jo961214v

  日期：1996.1.1

  The substrate specificity and enzymatic sialylation ability of the bacterium alpha-2,6-sialyltransferase were examined. The enzyme assay displayed a remarkable ability to catalyze sialyl transfer to type-II oligosaccharides possessing fucoside or sialoside at the 2 or 3 position of the terminal galactoside. Enzymatic syntheses were performed in order to confirm the structure of unusual assay products found when using Neu5Ac beta 2,3Gal beta 1,4Glc and Fuc alpha 1,2Gal beta 1,4Glc as the sialyl accepters. Both sialylation reactions (10 mu mol scales) were run using 83 munits of enzyme, were complete in 2 h, and afforded the sialoside analogues Neu5Ac alpha 2,6(Fuc alpha 1,2) Gal beta 1,4Glc (88%) and Neu5Ac alpha 2,6(Neu5Ac beta 2,3) Gal beta 1,4Glc (92%).