glycyrrhetic acid 3-O-glucuronide

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: glycyrrhetic acid 3-O-glucuronide
• 英文别名: GAMG；(2S,3S,4S,5R,6S)-6-[[(3S,4aR,6aR,6bS,8aS,11S,12aR,14aR,14bS)-11-carboxy-4,4,6a,6b,8a,11,14b-heptamethyl-14-oxo-2,3,4a,5,6,7,8,9,10,12,12a,14a-dodecahydro-1H-picen-3-yl]oxy]-3,4,5-trihydroxyoxane-2-carboxylic acid
• 化学式: C₃₆H₅₄O₁₀
• 分子量: 646.819
• InChiKey: HLDYLAJAWSKPFZ-HBKAJLBFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.1
• 重原子数：
  46
• 可旋转键数：
  4
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  171
• 氢给体数：
  5
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  甘草酸 在 biotinylated β-glucuronidase from E. coli conjugated on asymmetric temperature responsive polyurethane 作用下， 以 aq. phosphate buffer 为溶剂， 反应 24.0h， 以33%的产率得到glycyrrhetic acid 3-O-glucuronide
  参考文献：
  名称：

  Thermally controlled biotransformation of glycyrrhizic acidviaan asymmetric temperature-responsive polyurethane membrane

  摘要：

  一种“智能”生物反应系统是通过利用温度响应性聚氨酯（TRPU）的特殊特性而开发的。这种“智能”支撑材料为复杂的生物转化反应提供了分离的潜在好处。

  DOI：

  10.1039/c8ra06202a

文献信息

• Bacteroides J-37, a Human Intestinal Bacterium, Produces .ALPHA.-Glucuronidase.
  作者：Dong-Hyun KIM、Il-Sung JANG、Seung-Won LEE

  DOI：10.1248/bpb.20.834

  日期：——

  β-Glucuronidases of mammalian tissues metabolized glycyrrhizin (18β-glycyrrhetinic acid, β-D-glucuronyl α-D-glucuronic acid, GL) to glycyrrhetinic acid (GA) via 18β-glycyrrhetinic acid α-D-glucuronic acid (GAMG); they hydrolyzed β-glucuronic acid conjugates better than α-glucuronic acid conjugates. However, human intestinal bacteria directly metabolized GL to GA, and minorly to GA via GAMG. Bacteroides J-37, isolated from human intestinal bacteria, transformed GL or GAMG to GA, but not baicalin; it produced α-glucuroniase, which hydrolyzed the α-linkage of glucuronic acid conjugates. α-Glucuronidase of Bacteroides J-37 hydrolyzed α-glucuronic acid conjugates better than β-glucuronic acid conjugates. β-Glucuronidase from E. coli, a human intestinal bacterium, hydrolyzed baicalin to baicalein, but did not transform GL.

  哺乳动物组织的β-葡萄糖醛酸酶通过18β-甘草次酸α-D-葡萄糖醛酸（GAMG）将甘草甜素（18β-甘草次酸、β-D-葡萄糖醛酸基α-D-葡萄糖醛酸，GL）代谢为甘草次酸（GA）；它们对 β-葡萄糖醛酸结合物的水解效果优于 α-葡萄糖醛酸结合物。然而，人类肠道细菌直接将GL代谢为GA，少量通过GAMG代谢为GA。从人类肠道细菌中分离出的 Bacteroides J-37 将 GL 或 GAMG 转化为 GA，但黄芩苷不转化；它产生α-葡萄糖醛酸酶，水解葡萄糖醛酸缀合物的α-键。拟杆菌 J-37 的 α-葡萄糖醛酸酶比 β-葡萄糖醛酸缀合物更好地水解 α-葡萄糖醛酸缀合物。来自大肠杆菌（一种人类肠道细菌）的 β-葡萄糖醛酸酶将黄芩苷水解为黄芩素，但不转化 GL。
• Muro, Tetsuo; Kuramoto, Takashi; Imoto, Katsue, Agricultural and Biological Chemistry, 1986, vol. 50, # 3, p. 687 - 692
  作者：Muro, Tetsuo、Kuramoto, Takashi、Imoto, Katsue、Okada, Shigetaka

  DOI：——

  日期：——
• Purification and characterization of a highly selective glycyrrhizin-hydrolyzing β-glucuronidase from Penicillium purpurogenum Li-3
  作者：Shuping Zou、Guiyan Liu、Imdad Kaleem、Chun Li

  DOI：10.1016/j.procbio.2012.12.008

  日期：2013.2

  A novel beta-glucuronidase from filamentous fungus Penicillium purpurogenum Li-3 was purified to electrophoretic homogeneity by ultrafiltration, ammonium sulfate precipitation, DEAE-cellulose ion exchange chromatography, and Sephadex G-100 gel filtration with an 80.7-fold increase in specific activity. The purified beta-glucuronidase is a dimeric protein with an apparent molecular mass of 69.72 kDa (m/z=69,717), determined by MALDI/TOF-MS. The optimal temperature and pH of the purified enzyme are 40 degrees C and 6.0, respectively. The enzyme is stable within pH 5.0-8.0, and the temperature up to 45 degrees C. Mg2+ ions enhanced the activity of the enzyme, Ca2+ and Al3+ showed no effect, while Mn2+, Zn2+, Hg2+ and Cu2+ substantially inhibited the enzymatic activity. The K-m and V-max values of the purified enzyme for glycyrrhizin (GL) were evaluated as 0.33 mM and 59.0 mmol mg(-1) min(-1), respectively. The purified enzyme displayed a highly selective glycyrrhizin-hydrolyzing property and converted GL directly to glycyrrhetic acid mono-glucuronide (GAMG), without producing byproduct glycyrrhetic acid (GA). The results suggest that the purified enzyme may have potential applications in bio-pharmaceutical and biotechnological industry. (C) 2013 Elsevier Ltd. All rights reserved.