phenacyl (5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronate | 374105-90-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: phenacyl (5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronate
• 英文别名: phenacyl (2R,3S,4R,5R,6S)-3,4,5-triacetyloxy-2,6-difluorooxane-2-carboxylate
• CAS: 374105-90-5
• 化学式: C₂₀H₂₀F₂O₁₀
• 分子量: 458.37
• InChiKey: KKPZZSRELFGFPQ-NUABRCLCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  32
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  132
• 氢给体数：
  0
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  phenacyl (5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronate 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 、 水 为溶剂， 反应 1.0h， 以90%的产率得到(5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronic acid
  参考文献：
  名称：

  Synthesis of 5-fluoro-β-<SMALL>D</SMALL>-glucopyranosyluronic acid fluoride and its evaluation as a mechanistic probe of <i>Escherichia coli </i>β-glucuronidase

  摘要：

  Synthesis of the potential mechanism-based inactivator of beta -D-glucuronidases (5-fluoro-beta -D-glucopyranosyluronic acid fluoride) was accomplished via a six-step process from D-glucuronic acid that involved radical bromination at C-5 and displacement of the bromide by fluoride. A key step in this process was the masking of the carboxylic acid as a phenacyl ester. This group is uniquely stable to conditions of photobromination and fluoride displacement, yet removable under very mild conditions. Incubation of the Escherichia coli beta -glucuronidase with 5-fluoro-beta -D-glucopyranosyluronic acid fluoride resulted in time-dependent inactivation of the enzyme through the accumulation of a covalent 5-fluoro-alpha -D-glucopyranosyluronic acid-enzyme. Peptic digestion of the 5-fluoro-alpha -D-glucopyranosyluronic acid-enzyme intermediate and subsequent analysis by liquid chromatography coupled to an electrospray ionization triple quadrupole mass spectrometer indicated the presence of a 5-fluoro-alpha -D-glucopyranosyluronic acid-modified peptide. This peptide was partially purified by HPLC and its sequence determined by tandem mass spectrometry in the daughter ion scan mode, permitting the identification of Glu504 as the catalytic nucleophile within the sequence ITEYGVD. This new reagent is therefore useful for the specific, mechanism-based inactivation of glycuronidases and has good potential in other studies of enzymes of this general class.

  DOI：

  10.1139/cjc-79-5-6-510
• 作为产物：
  描述：

  phenacyl (2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronate 在 N-溴代丁二酰亚胺(NBS) 、 silver tetrafluoroborate 作用下， 以 四氯化碳 、 乙醚 为溶剂， 反应 3.0h， 生成 phenacyl (5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronate
  参考文献：
  名称：

  Synthesis of 5-fluoro-β-<SMALL>D</SMALL>-glucopyranosyluronic acid fluoride and its evaluation as a mechanistic probe of <i>Escherichia coli </i>β-glucuronidase

  摘要：

  Synthesis of the potential mechanism-based inactivator of beta -D-glucuronidases (5-fluoro-beta -D-glucopyranosyluronic acid fluoride) was accomplished via a six-step process from D-glucuronic acid that involved radical bromination at C-5 and displacement of the bromide by fluoride. A key step in this process was the masking of the carboxylic acid as a phenacyl ester. This group is uniquely stable to conditions of photobromination and fluoride displacement, yet removable under very mild conditions. Incubation of the Escherichia coli beta -glucuronidase with 5-fluoro-beta -D-glucopyranosyluronic acid fluoride resulted in time-dependent inactivation of the enzyme through the accumulation of a covalent 5-fluoro-alpha -D-glucopyranosyluronic acid-enzyme. Peptic digestion of the 5-fluoro-alpha -D-glucopyranosyluronic acid-enzyme intermediate and subsequent analysis by liquid chromatography coupled to an electrospray ionization triple quadrupole mass spectrometer indicated the presence of a 5-fluoro-alpha -D-glucopyranosyluronic acid-modified peptide. This peptide was partially purified by HPLC and its sequence determined by tandem mass spectrometry in the daughter ion scan mode, permitting the identification of Glu504 as the catalytic nucleophile within the sequence ITEYGVD. This new reagent is therefore useful for the specific, mechanism-based inactivation of glycuronidases and has good potential in other studies of enzymes of this general class.

  DOI：

  10.1139/cjc-79-5-6-510