(5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronic acid | 374105-92-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronic acid
• 英文别名: (2R,3S,4R,5R,6S)-3,4,5-triacetyloxy-2,6-difluorooxane-2-carboxylic acid
• CAS: 374105-92-7
• 化学式: C₁₂H₁₄F₂O₉
• 分子量: 340.235
• InChiKey: YCEOQFNXRHCOCE-GPTQDWHKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  23
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  125
• 氢给体数：
  1
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  (5-fluoro-2,3,4-tri-O-acetyl-β-D-glucopyranosyl fluoride)uronic acid 在 氨 作用下， 以 甲醇 为溶剂， 反应 0.5h， 以85%的产率得到(5-fluoro-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：

  D-吡喃葡萄糖醛酸 在 palladium on activated charcoal N-溴代丁二酰亚胺(NBS) 、 silver tetrafluoroborate 、 硫酸 、 氢气 、 乙酸肼 、 4,4'-二氨基二苯乙烯-2,2'-二磺酸 作用下， 以 甲醇 、 四氯化碳 、 乙醚 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 20.0h， 生成 (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

文献信息

• Synthesis of 5-fluoro-β-&lt;SMALL&gt;D&lt;/SMALL&gt;-glucopyranosyluronic acid fluoride and its evaluation as a mechanistic probe of &lt;i&gt;Escherichia coli &lt;/i&gt;β-glucuronidase
  作者：Alexander W. Wong、Shouming He、Stephen G. Withers

  DOI：10.1139/cjc-79-5-6-510

  日期：——

  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.