benzyl 2-acetamido-4-azido-2,4-deoxy-β-D-glucopyranoside | 159234-88-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: benzyl 2-acetamido-4-azido-2,4-deoxy-β-D-glucopyranoside
• 英文别名: N-[(2R,3R,4R,5S,6S)-5-azido-4-hydroxy-6-(hydroxymethyl)-2-phenylmethoxyoxan-3-yl]acetamide
• CAS: 159234-88-5
• 化学式: C₁₅H₂₀N₄O₅
• 分子量: 336.348
• InChiKey: SQUQZDKLBHFVGC-ARILJUKYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  24
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  102
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  benzyl 2-acetamido-4-azido-2,4-deoxy-β-D-glucopyranoside 在 palladium dihydroxide 吡啶 、 palladium dihydroxide 、 氢气 、 sodium methylate 、 N,N-二异丙基乙胺 、 sodium iodide 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 甲醇 、 乙腈 为溶剂， 反应 20.17h， 生成 dibenzylphospho-2,4-acetamido-3-O-benzoyl-2,4,6-deoxy-α-D-glucopyranoside
  参考文献：
  名称：

  Investigating Bacterial N-Linked Glycosylation:  Synthesis and Glycosyl Acceptor Activity of the Undecaprenyl Pyrophosphate-Linked Bacillosamine

  摘要：

  The chemical synthesis and biological activity of undecaprenyl pyrophosphate bacillosamine (Und-PP-Bac), an obligatory intermediate in the asparagine-linked glycosylation pathway of Campylobacter jejuni, are reported. The key transformation involves the coupling of bacillosamine phosphate and undecaprenyl phosphate. The synthetic Und-PP-Bac can be used to investigate the activity of the enzyme PglA, which catalyzes the first glycosyl transfer in substrate biosynthesis for N-linked protein glycosylation in the pathogenic gram-negative bacterium. The availability of this synthetic substrate makes it possible to access polyprenyl-linked oligosaccharides, such as the GalNAc-alpha-1,3-bacillosamine-alpha-1-PP-Und intermediate, that will enable exploration of the remaining enzymes in the prokaryotic glycosylation pathway. Study of the bacterial glycosylation system will provide insight into the corresponding eukaryotic process, which is currently poorly understood.

  DOI：

  10.1021/ja054265v
• 作为产物：
  描述：

  benzyl 2-acetamido-3,6-di-O-benzoyl-2-deoxy-β-D-galactopyranoside 在 吡啶 、 sodium azide 、 sodium methylate 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 生成 benzyl 2-acetamido-4-azido-2,4-deoxy-β-D-glucopyranoside
  参考文献：
  名称：

  Investigating Bacterial N-Linked Glycosylation:  Synthesis and Glycosyl Acceptor Activity of the Undecaprenyl Pyrophosphate-Linked Bacillosamine

  摘要：

  The chemical synthesis and biological activity of undecaprenyl pyrophosphate bacillosamine (Und-PP-Bac), an obligatory intermediate in the asparagine-linked glycosylation pathway of Campylobacter jejuni, are reported. The key transformation involves the coupling of bacillosamine phosphate and undecaprenyl phosphate. The synthetic Und-PP-Bac can be used to investigate the activity of the enzyme PglA, which catalyzes the first glycosyl transfer in substrate biosynthesis for N-linked protein glycosylation in the pathogenic gram-negative bacterium. The availability of this synthetic substrate makes it possible to access polyprenyl-linked oligosaccharides, such as the GalNAc-alpha-1,3-bacillosamine-alpha-1-PP-Und intermediate, that will enable exploration of the remaining enzymes in the prokaryotic glycosylation pathway. Study of the bacterial glycosylation system will provide insight into the corresponding eukaryotic process, which is currently poorly understood.

  DOI：

  10.1021/ja054265v

文献信息

• Investigating Bacterial N-Linked Glycosylation:  Synthesis and Glycosyl Acceptor Activity of the Undecaprenyl Pyrophosphate-Linked Bacillosamine
  作者：Eranthie Weerapana、Kerney Jebrell Glover、Mark M. Chen、Barbara Imperiali

  DOI：10.1021/ja054265v

  日期：2005.10.1

  The chemical synthesis and biological activity of undecaprenyl pyrophosphate bacillosamine (Und-PP-Bac), an obligatory intermediate in the asparagine-linked glycosylation pathway of Campylobacter jejuni, are reported. The key transformation involves the coupling of bacillosamine phosphate and undecaprenyl phosphate. The synthetic Und-PP-Bac can be used to investigate the activity of the enzyme PglA, which catalyzes the first glycosyl transfer in substrate biosynthesis for N-linked protein glycosylation in the pathogenic gram-negative bacterium. The availability of this synthetic substrate makes it possible to access polyprenyl-linked oligosaccharides, such as the GalNAc-alpha-1,3-bacillosamine-alpha-1-PP-Und intermediate, that will enable exploration of the remaining enzymes in the prokaryotic glycosylation pathway. Study of the bacterial glycosylation system will provide insight into the corresponding eukaryotic process, which is currently poorly understood.