5-phenylpentyl β-D-glucopyranoside

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 5-phenylpentyl β-D-glucopyranoside
• 英文别名: (2R,3S,4S,5R,6R)-2-(hydroxymethyl)-6-(5-phenylpentoxy)oxane-3,4,5-triol
• 化学式: C₁₇H₂₆O₆
• 分子量: 326.39
• InChiKey: RDTNQDQALRQETG-NQNKBUKLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  23
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  99.4
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  5-phenylpentyl 2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside 在 Amberlite IRA-400 作用下， 以 甲醇 为溶剂， 反应 24.0h， 以94%的产率得到5-phenylpentyl β-D-glucopyranoside
  参考文献：
  名称：

  Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

  摘要：

  来自嗜热菌Pyrococcus furiosus的超热稳定β-葡萄糖苷酶通过与转谷氨酰胺酶交联封装在明胶凝胶中。明胶固定的β-葡萄糖苷酶比天然酶具有更高的热稳定性。冷冻干燥的固定化酶在90°C下储存1个月而不会丧失活性。固定化的β-葡萄糖苷酶在pH 5.0和70°C下催化5-苯基戊醇与10.0当量的纤维二糖进行转葡萄糖基作用12小时，生成5-苯基戊基-β-D-吡喃葡萄糖苷，产率为41%。固定化酶在转葡萄糖基作用中比天然酶更有效。从首次反应中回收的明胶固定的Pfu-β-葡萄糖苷酶可重复用于连续反应。

  DOI：

  10.1271/bbb.69.128

文献信息

• Simple Synthesis of .BETA.-D-Glycopyranosides Using .BETA.-Glycosidase from Almonds
  作者：Katsumi Kurashima、Mikio Fujii、Yoshiteru Ida、Hiroyuki Akita

  DOI：10.1248/cpb.52.270

  日期：——

  Enzymatic glycosidation of twenty-one kinds of alcohols (n-hepanol, n-octanol, 2-phenylethanol, 3-phenylpropanol, 4-phenylbutanol, 5-phenylpentanol, 6-phenylhexanol, furfury alcohol, 2-pyridinemethanol, isobutanol, isopentanol, p-methoxycinnamylalcohol) including secondary alcohols (isopropanol, cyclohexanol, 1-phenylethanol) and 1,ω-alkanediols (1,5-pentanediol, 1,6-hexanediol, 1,7-heptanediol, 1,8-octanediol, 1,9-nonanediol), salicyl alcohol and 4-nitrophenyl β-D-glucopyranoside (5) using β-glucosidase from almonds stereoselectively gave the corresponding β-D-glucopyranosides in moderate yield.

  酶促糖苷化反应对二十一种醇类（正庚醇、正辛醇、2-苯乙醇、3-苯丙醇、4-苯丁醇、5-苯戊醇、6-苯己醇、呋喃醇、2-吡啶甲醇、异丁醇、异戊醇、对甲氧基肉桂醇）进行，其中包括次级醇（异丙醇、环己醇、1-苯乙醇）和1,ω-烷二醇（1,5-戊二醇、1,6-己二醇、1,7-庚二醇、1,8-辛二醇、1,9-壬二醇），水杨醇及4-硝基苯基β-D-葡萄糖吡喃苷（5），使用来自杏仁的β-葡萄糖苷酶选择性地生成了相应的β-D-葡萄糖吡喃苷，产率适中。
• Preparation and Properties of Gelatin-Immobilized β-Glucosidase from<i>Pyrococcus furiosus</i>
  作者：Hidetaka NAGATOMO、Yoh-ichi MATSUSHITA、Kazuhiro SUGAMOTO、Takanao MATSUI

  DOI：10.1271/bbb.69.128

  日期：2005.1

  Hyperthermostable β-glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase. Gelatin-immobilized β-glucosidase was considerably more thermostable than the native enzyme. Lyophilized immobilisate was stored at 90 °C for 1 month without loss of activity. The immobilized β-glucosidase catalyzed transglucosylation of 5-phenylpentanol with 10.0 equivalent of cellobiose at pH 5.0 and 70 °C for 12 h to afford 5-phenylpentyl β-D-glucopyranoside in 41% yield. The immobilized enzyme was more effective than the native one in transglucosylation. The gelatin-immobilized Pfu-β-glucosidase recovered from the first run of the reaction was reusable on successive runs.

  来自嗜热菌Pyrococcus furiosus的超热稳定β-葡萄糖苷酶通过与转谷氨酰胺酶交联封装在明胶凝胶中。明胶固定的β-葡萄糖苷酶比天然酶具有更高的热稳定性。冷冻干燥的固定化酶在90°C下储存1个月而不会丧失活性。固定化的β-葡萄糖苷酶在pH 5.0和70°C下催化5-苯基戊醇与10.0当量的纤维二糖进行转葡萄糖基作用12小时，生成5-苯基戊基-β-D-吡喃葡萄糖苷，产率为41%。固定化酶在转葡萄糖基作用中比天然酶更有效。从首次反应中回收的明胶固定的Pfu-β-葡萄糖苷酶可重复用于连续反应。
• A variety of lipid-coated glycoside hydrolases as effective glycosyl transfer catalysts in homogeneous organic solvents
  作者：Toshiaki Mori、Yoshio Okahata

  DOI：10.1016/s0040-4039(97)00251-7

  日期：1997.3

  Various lipid-coated glycoside hydrolases were prepared, which act as efficient catalysts for transglycosylation of α-D- and β-D-mannoside, N-acetyl-β-D-glucosaminide, β-D-glucoside, and β-D-galactoside to hydrophobic acceptor alcohols in dry isopropyl ether. The enzyme activity for the glycosylation depended on coating lipids as well as origin or kind of enzymes.

  制备了各种脂质包覆的糖苷水解酶，它们可作为α-D-和β-D-甘露糖苷，N-乙酰基-β-D-氨基葡萄糖苷，β-D-葡萄糖苷和β-D-半乳糖苷转糖基化的有效催化剂在干燥的异丙醚中制得疏水性受体醇。糖基化的酶活性取决于包被的脂质以及酶的来源或种类。
• Rational Design of Glycomimetic Compounds Targeting the <i>Saccharomyces cerevisiae</i> Transglycosylase Gas2
  作者：Ignacio Delso、Jessika Valero‐González、Eduardo Marca、Tomás Tejero、Ramón Hurtado‐Guerrero、Pedro Merino

  DOI：10.1111/cbdd.12650

  日期：2016.2

  The transglycosylase Saccharomyces cerevisiae Gas2 (ScGas2) belongs to a large family of enzymes that are key players in yeast cell wall remodeling. Despite its biologic importance, no studies on the synthesis of substrate‐based compounds as potential inhibitors have been reported. We have synthesized a series of docking‐guided glycomimetics that were evaluated by fluorescence spectroscopy and saturation‐transfer difference (STD) NMR experiments, revealing that a minimum of three glucose units linked via a β‐(1,3) linkage are required for achieving molecular recognition at the binding donor site. The binding mode of our compounds is further supported by STD‐NMR experiments using the active site‐mutants Y107Q and Y244Q. Our results are important for both understanding of ScGas2–substrate interactions and setting up the basis for future design of glycomimetics as new antifungal agents.