fluorescein methyl ester mono(2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside) | 1395879-35-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: fluorescein methyl ester mono(2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside)
• 英文别名: methyl 2-[3-oxo-6-[(2S,3R,4S,5R,6R)-3,4,5-triacetyloxy-6-(acetyloxymethyl)oxan-2-yl]oxyxanthen-9-yl]benzoate
• CAS: 1395879-35-2
• 化学式: C₃₅H₃₂O₁₄
• 分子量: 676.631
• InChiKey: HQFOBXNMAUFZTA-DCLAJFSGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  49
• 可旋转键数：
  14
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  176
• 氢给体数：
  0
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  fluorescein methyl ester mono(2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside) 在 甲醇 、 sodium 作用下， 反应 2.0h， 以56%的产率得到fluorescein methyl ester mono(β-D-glucopyranoside)
  参考文献：
  名称：

  Monogalactopyranosides of fluorescein and fluorescein methyl ester: synthesis, enzymatic hydrolysis by biotnylated β-galactosidase, and determination of translational diffusion coefficient

  摘要：

  Fluorescein monoglycosides (D-galactopyranoside (FMG) and D-glucopyranoside) and their methyl ester (MFMG) have been prepared from acetobromoglucose/galactose and fluorescein methyl ester in good yields. Enzymatic hydrolysis experiments (using biotinylated beta-galactosidase) of the galacto derivatives have been performed and kinetic parameters were calculated. A 15-20 times increase of the fluorescence intensity has been observed during the hydrolysis. A linear increase of fluorescence has been noted at short time and low concentration of substrate, making these compounds useful and sensitive probes for galactosidases. The magnitude of the Michaelis-Menten constant (K-m) value for MFMG is higher than that of FMG suggesting a possible conformational change of the fluorogenic substrate. K-m value for biotinylated beta-Gal with FMG is lower than that for the native enzyme. This observation indicates higher substrate affinity of the biotinylated enzyme in comparison to the native enzyme. Translational diffusion coefficients have been measured, for both fluorogenic substrates and both the products, employing fluorescence correlation spectroscopy. Translational diffusion coefficients for fluorogenic substrates and the enzymatic hydrolysis products have been measured to be similar, in the range of 3.5-4.5 x 10(-10) m(2) s(-1). Thus an enhancement or retardation of the enzymatic kinetics due to difference in translational mobility of substrate and product is not that apparent. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2012.05.017
• 作为产物：
  描述：

  荧光素甲酯 、 2,3,4,6-四乙酰氧基-alpha-D-吡喃葡萄糖溴化物 在 caesium carbonate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 5.0h， 以72%的产率得到fluorescein methyl ester mono(2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside)
  参考文献：
  名称：

  Monogalactopyranosides of fluorescein and fluorescein methyl ester: synthesis, enzymatic hydrolysis by biotnylated β-galactosidase, and determination of translational diffusion coefficient

  摘要：

  Fluorescein monoglycosides (D-galactopyranoside (FMG) and D-glucopyranoside) and their methyl ester (MFMG) have been prepared from acetobromoglucose/galactose and fluorescein methyl ester in good yields. Enzymatic hydrolysis experiments (using biotinylated beta-galactosidase) of the galacto derivatives have been performed and kinetic parameters were calculated. A 15-20 times increase of the fluorescence intensity has been observed during the hydrolysis. A linear increase of fluorescence has been noted at short time and low concentration of substrate, making these compounds useful and sensitive probes for galactosidases. The magnitude of the Michaelis-Menten constant (K-m) value for MFMG is higher than that of FMG suggesting a possible conformational change of the fluorogenic substrate. K-m value for biotinylated beta-Gal with FMG is lower than that for the native enzyme. This observation indicates higher substrate affinity of the biotinylated enzyme in comparison to the native enzyme. Translational diffusion coefficients have been measured, for both fluorogenic substrates and both the products, employing fluorescence correlation spectroscopy. Translational diffusion coefficients for fluorogenic substrates and the enzymatic hydrolysis products have been measured to be similar, in the range of 3.5-4.5 x 10(-10) m(2) s(-1). Thus an enhancement or retardation of the enzymatic kinetics due to difference in translational mobility of substrate and product is not that apparent. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2012.05.017