1-O-(p-nitrophenyl)-[β-D-glucuronyl-(1->3)]-β-D-glucuronic acid

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 1-O-(p-nitrophenyl)-[β-D-glucuronyl-(1->3)]-β-D-glucuronic acid
• 英文别名: β-D-GlcA-(1->3)-β-D-GlcA-O-pNP；GlcA(b1-3)GlcA(b)-O-Ph(4-NO2)；(2S,3S,4S,5R,6R)-6-[(2S,3S,4S,5R,6S)-2-carboxy-3,5-dihydroxy-6-(4-nitrophenoxy)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid
• 化学式: C₁₈H₂₁NO₁₅
• 分子量: 491.362
• InChiKey: WOONYVSKNMDRQC-BTNCTRPFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.5
• 重原子数：
  34
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  259
• 氢给体数：
  7
• 氢受体数：
  15

反应信息

• 作为产物：
  描述：

  4-硝基苯-Β-D-葡萄糖苷酸 在 碳酸氢钠 作用下， 以 acetate buffer 为溶剂， 反应 24.0h， 以10 mg的产率得到1-O-(p-nitrophenyl)-[β-D-glucuronyl-(1->3)]-β-D-glucuronic acid
  参考文献：
  名称：

  A bovine glucuronidase for assembly of β-d-glucuronyl-(1–3)-6-O-sulfo-β-d-gluco- and galacto-pyranosyl linkages

  摘要：

  通过使用 4-硝基苯δ-D-葡萄糖醛酸（D-GlcA-O-pNP）作为糖基供体，研究了葡萄糖醛酸酶催化的转糖基化作用；当使用 pNP 6-O-磺酰基-δ-D-吡喃葡萄糖苷和 D-半乳糖苷作为受体时，发现一种牛酶能以位点选择性和δ选择性的方式与 6-O-磺酰基糖构建δ-D-GlcA-(1â3)-连接。

  DOI：

  10.1039/b516921f

文献信息

• A bovine glucuronidase for assembly of β-d-glucuronyl-(1–3)-6-O-sulfo-β-d-gluco- and galacto-pyranosyl linkages
  作者：Hirotaka Uzawa、Takehiro Nagatsuka、Hideo Hiramatsu、Yoshihiro Nishida

  DOI：10.1039/b516921f

  日期：——

  Glucuronidase-catalyzed transglycosylation was examined by using 4-nitrophenyl β-D-glucuronide (D-GlcA-O-pNP) as the glycosyl donor; when pNP 6-O-sulfo-β-D-gluco- and D-galacto-pyranosides were used as the acceptors, a bovine enzyme was found to construct β-D-GlcA-(1–3)-linkages with the 6-O-sulfo-sugars in both a site- and β-selective way.

  通过使用 4-硝基苯δ-D-葡萄糖醛酸（D-GlcA-O-pNP）作为糖基供体，研究了葡萄糖醛酸酶催化的转糖基化作用；当使用 pNP 6-O-磺酰基-δ-D-吡喃葡萄糖苷和 D-半乳糖苷作为受体时，发现一种牛酶能以位点选择性和δ选择性的方式与 6-O-磺酰基糖构建δ-D-GlcA-(1â3)-连接。
• Glucuronidase-assisted Transglycosylation for the Synthesis of Highly Functional Disaccharides: β-D-Glucuronyl 6-<i>O</i>-Sulfo-β-D-Gluco- and -β-D-Galactopyranosides
  作者：Takehiro Nagatsuka、Hirotaka Uzawa、Hiroyuki Asanuma、Yoshihiro Nishida

  DOI：10.1080/07328300802696215

  日期：2009.2.27

  The substrate specificity of snail (Helix pomatia and Helix aspersa), limpet (Patella vulgata), and bovine glucuronidases was examined by using p-nitrophenyl glucuronide (GlcA-O-pNP) and p-nitrophenyl 6-O-sulfo--D-glycopyranosides as the glycosyl donor and acceptors, respectively. When the donor was treated with these enzymes in the absence of the acceptors, (1 3) glucuronyl disaccharides were obtained as the major products together with (1 2) isomers as the result of an enzymatic self-transglycosylation reaction. When p-nitrophenyl 6-O-sulfo--D-glucopyranosides (6-O-sulfo-Glc-O-pNP and 6-O-sulfo-Glc-S-pNP) were applied as acceptor substrates, every glucuronidase transferred the GlcA residue to either the O-3 or O-2 position in 6-O-sulfo-Glc to yield a mixture of GlcA (1 3)- and GlcA (1 2)-linked disaccharides in a ratio of 12:1 1:1. On the other hand, when p-nitrophenyl 6-O-sulfo--D-galactopyranosides (6-O-sulfo-Gal-O-pNP and 6-O-sulfo-Gal-S-pNP) were applied, limpet and bovine glucuronidases gave a GlcA (1 3)-linked disaccharide regioselectively, while the snail enzymes showed no reactivity.