methyl 2-acetamido-2-deoxy-3-O-benzyl-4-O-(3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside | 440345-41-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: methyl 2-acetamido-2-deoxy-3-O-benzyl-4-O-(3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside
• 英文别名: Bn(-3)[Bn(-4)][Bn(-6)]Gal(b1-4)[Bn(-3)]b-GlcNAc1Me；N-[(2R,3R,4R,5S,6R)-5-[(2S,3R,4R,5S,6R)-3-hydroxy-4,5-bis(phenylmethoxy)-6-(phenylmethoxymethyl)oxan-2-yl]oxy-6-(hydroxymethyl)-2-methoxy-4-phenylmethoxyoxan-3-yl]acetamide
• CAS: 440345-41-5
• 化学式: C₄₃H₅₁NO₁₁
• 分子量: 757.878
• InChiKey: XYSLKZLDCGQMRK-LFYSUEOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  55
• 可旋转键数：
  18
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  143
• 氢给体数：
  3
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  methyl 2-acetamido-2-deoxy-3-O-benzyl-4-O-(3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 在 10percent Pd/C 吡啶 、 氢气 、 sodium hydride 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 55.5h， 生成 methyl 2-acetamido-2-deoxy-4-O-(β-D-galactopyranosyl)-2',6-di-O-(ethane-1,2-diyl)-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：

  O-(2-O-Acetyl-3,4,6-tri-O-benzyl-α-D-galactopyranosyl) trichloroacetimidate 在 甲醇 、 三氟化硼乙醚 、 sodium methylate 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 51.08h， 生成 methyl 2-acetamido-2-deoxy-3-O-benzyl-4-O-(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

文献信息

• Glycosyltransferase activity can be selectively modulated by chemical modifications of acceptor substrates
  作者：M.Carmen Galan、Christopher S Dodson、Andre P Venot、Geert-Jan Boons

  DOI：10.1016/j.bmcl.2004.02.024

  日期：2004.5

  A range of N-acetyllactosamine derivatives, which are modified by a wide range of functionalities at C-2' and C-6, have been synthesised and the kinetic parameters of transfer catalysed by recombinant alpha-2,6-sialyltransferase and alpha-1,3-fucoyltransferase VI determined. Several of the chemical modifications led to selective modulate the activity the enzymes and offer promising lead compounds for the development of oligosaccharide primers for selective metabolic inhibition of oligosaccharide biosynthesis. (C) 2004 Elsevier Ltd. All rights reserved.
• 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.