2-acetamido-2-deoxy-α-D-glucopyranosyl 11-phenoxyundecyl malonate | 1147646-76-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-acetamido-2-deoxy-α-D-glucopyranosyl 11-phenoxyundecyl malonate
• 英文别名: GlcNAcα-malonate-(CH2)11-O-Ph；3-O-[(2R,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] 1-O-(11-phenoxyundecyl) propanedioate
• CAS: 1147646-76-1
• 化学式: C₂₈H₄₃NO₁₀
• 分子量: 553.65
• InChiKey: SSUKKJPRIXOZQJ-DVVXUNHVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  39
• 可旋转键数：
  20
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  161
• 氢给体数：
  4
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  3,4,6-tri-O-benzyl-2-acetamido-2-deoxy-α-D-glucopyranosyl 11-phenoxyundecyl malonate 在 palladium 10% on activated carbon 、 氢气 作用下， 以 甲醇 为溶剂， 反应 16.0h， 以92%的产率得到2-acetamido-2-deoxy-α-D-glucopyranosyl 11-phenoxyundecyl malonate
  参考文献：
  名称：

  Synthesis of acceptor substrate analogs for the study of glycosyltransferases involved in the second step of the biosynthesis of O-antigen repeating units

  摘要：

  O-antigens of Gram negative bacteria are polysaccharides covalently attached to lipopolysaccharides (LPS) that have roles as virulence factors. Due to the lack of defined substrates for in vitro assays only a few of the enzymes involved in the biosynthesis of O-antigens have been studied. Many O-antigens have GlcNAc at the reducing end of the oligosaccharide chain linked to pyrophosphate-lipid. We therefore designed and synthesized a series of GlcNAc-pyrophosphate-lipid analogs of the natural GlcNAc-pyrophosphate-undecaprenol acceptor substrate for studies of the acceptor specificities of O-antigen biosynthetic enzymes. We synthesized analogs with modifications of the pyrophosphate bond as well as the lipid chain. These compounds will be useful for the specificity studies of many bacterial glycosyltransferases. Knowledge of the substrate specificities is the basis for the development of specific glycosyltransferase inhibitors that could block O-antigen biosynthesis. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2009.12.022

文献信息

• Synthesis of acceptor substrate analogs for the study of glycosyltransferases involved in the second step of the biosynthesis of O-antigen repeating units
  作者：John G. Riley、Changchang Xu、Inka Brockhausen

  DOI：10.1016/j.carres.2009.12.022

  日期：2010.3

  O-antigens of Gram negative bacteria are polysaccharides covalently attached to lipopolysaccharides (LPS) that have roles as virulence factors. Due to the lack of defined substrates for in vitro assays only a few of the enzymes involved in the biosynthesis of O-antigens have been studied. Many O-antigens have GlcNAc at the reducing end of the oligosaccharide chain linked to pyrophosphate-lipid. We therefore designed and synthesized a series of GlcNAc-pyrophosphate-lipid analogs of the natural GlcNAc-pyrophosphate-undecaprenol acceptor substrate for studies of the acceptor specificities of O-antigen biosynthetic enzymes. We synthesized analogs with modifications of the pyrophosphate bond as well as the lipid chain. These compounds will be useful for the specificity studies of many bacterial glycosyltransferases. Knowledge of the substrate specificities is the basis for the development of specific glycosyltransferase inhibitors that could block O-antigen biosynthesis. (C) 2010 Elsevier Ltd. All rights reserved.