p-nitrophenyl β-D-galactopyranoside | 39031-76-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: p-nitrophenyl β-D-galactopyranoside
• 英文别名: p-nitrophenyl β-D-galactopyranosiduronic acid；p-nitrophenyl-2,3,4-tri-O-acetyl-beta-D-galacturonic acid；p-Nitrophenyl-β-D-galacturonsaeure；p-Nitrophenyl beta-D-galacturonide；(2S,3R,4S,5R,6S)-3,4,5-trihydroxy-6-(4-nitrophenoxy)oxane-2-carboxylic acid
• CAS: 39031-76-0
• 化学式: C₁₂H₁₃NO₉
• 分子量: 315.237
• InChiKey: QSUILVWOWLUOEU-TYCYOEEFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  22
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.416
• 拓扑面积：
  162
• 氢给体数：
  4
• 氢受体数：
  9

安全信息

• WGK Germany：
  3

反应信息

• 作为反应物：
  描述：

  p-nitrophenyl β-D-galactopyranoside 在 serAnGlc*of*Aspergillus*niger*van*Tieghem*(ATCC*22343) 作用下， 以 acetate buffer 为溶剂， 生成 D-吡喃葡萄糖醛酸
  参考文献：
  名称：

  Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein

  摘要：

  The carbohydrate moieties of arabinogalactan-proteins (AGPs), which are mainly composed of Gal, L-Ara, GlcA, and 4Me-GlcA residues, are essential for the physiological functions of these proteoglycans in higher plants. For this study, we have identified two genes encoding family 79 beta-glueuronidases, designated AnGlcAase and NcGlcAase, in Aspergillus niger and Neurospora crassa, respectively, based on the amino acid sequence of a native beta-glucuronidase purified from a commercial pectolytic enzyme preparation from A. niger. Although the deduced protein sequences of AnGlcAase and NcGlcAase were highly similar, the recombinant enzymes expressed in Pichia pastoris exhibited distinct substrate specificity toward 4-Me-GlcA residues of AGPs: recombinant ADGlcAase (rAnGlcAase) substantially liberated both GlcA and 4-Me-GlcA residues from radish AGPs, whereas recombinant NcGlcAase (rNcGlcAase) activity on the 4-Me-GlcA residues of AGPs was very low. Maximum activity of rAnGlcAase hydrolyzing PNP beta-GlcA occurred at pH 3.0-4.0, whereas the maximum rNcGlcAase activity was at pH 6.0. The apparent K. values of rAnGlcAase were 30.4 mu M for PNP beta-GlcA and 422 mu M for beta-GIcA-(1 -> 6)-Gal, and those of rNcGlcAase were 38.3 mu M and 378 mu M, respectively. Similar to the native enzyme, rAnGlcAase was able to catalyze the transglycosylation of GlcA residues from PNP beta-GlcA to various monosaccharide acceptors such as Glc, Gal, and Xyl. We propose that both AnGlcAase and NcGlcAase are instances of a novel type of beta-glucuronidase with the capacity to hydrolyze beta-GlcA and 4-Me-beta-GlcA residues of AGPs, although they differ significantly in their preferences. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2008.03.004
• 作为产物：
  描述：

  methyl (2,3,4-tri-O-acetyl-α-D-galactopyranosyl bromide)uronate 在 甲醇 、 碘 、 silver carbonate 、 lithium hydroxide 作用下， 以 二氯甲烷 为溶剂， 反应 28.17h， 生成 p-nitrophenyl β-D-galactopyranoside
  参考文献：
  名称：

  一种取代苄基或取代苯基β-D-己糖醛酸糖苷 的制备方法

  摘要：

  本发明涉及医药化工技术领域，公开了一种取代苄基或取代苯基β‑D‑己糖醛酸糖苷的制备方法，以己糖醛酸为原料，经乙酰化、选择性脱酰基、甲酯化、溴代、成醚、碱性醇解得取代苄基或取代苯基β‑己糖醛酸糖苷，结构式如下：I；其中，n＝0，1；R为邻、间或对位的氢、硝基、甲氧基或卤素。本反应条件温和，步骤简单，反应试剂易得，适合于大规模制备。

  公开号：

  CN108610386B

文献信息

• 一种取代苄基或取代苯基β-D-己糖醛酸糖苷 的制备方法
  申请人：上海交通大学

  公开号：CN108610386B

  公开（公告）日：2020-11-24

  本发明涉及医药化工技术领域，公开了一种取代苄基或取代苯基β‑D‑己糖醛酸糖苷的制备方法，以己糖醛酸为原料，经乙酰化、选择性脱酰基、甲酯化、溴代、成醚、碱性醇解得取代苄基或取代苯基β‑己糖醛酸糖苷，结构式如下：I；其中，n＝0，1；R为邻、间或对位的氢、硝基、甲氧基或卤素。本反应条件温和，步骤简单，反应试剂易得，适合于大规模制备。
• Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein
  作者：Tomoyuki Konishi、Toshihisa Kotake、Dina Soraya、Koji Matsuoka、Tetsuo Koyama、Satoshi Kaneko、Kiyohiko Igarashi、Masahiro Samejima、Yoichi Tsumuraya

  DOI：10.1016/j.carres.2008.03.004

  日期：2008.5

  The carbohydrate moieties of arabinogalactan-proteins (AGPs), which are mainly composed of Gal, L-Ara, GlcA, and 4Me-GlcA residues, are essential for the physiological functions of these proteoglycans in higher plants. For this study, we have identified two genes encoding family 79 beta-glueuronidases, designated AnGlcAase and NcGlcAase, in Aspergillus niger and Neurospora crassa, respectively, based on the amino acid sequence of a native beta-glucuronidase purified from a commercial pectolytic enzyme preparation from A. niger. Although the deduced protein sequences of AnGlcAase and NcGlcAase were highly similar, the recombinant enzymes expressed in Pichia pastoris exhibited distinct substrate specificity toward 4-Me-GlcA residues of AGPs: recombinant ADGlcAase (rAnGlcAase) substantially liberated both GlcA and 4-Me-GlcA residues from radish AGPs, whereas recombinant NcGlcAase (rNcGlcAase) activity on the 4-Me-GlcA residues of AGPs was very low. Maximum activity of rAnGlcAase hydrolyzing PNP beta-GlcA occurred at pH 3.0-4.0, whereas the maximum rNcGlcAase activity was at pH 6.0. The apparent K. values of rAnGlcAase were 30.4 mu M for PNP beta-GlcA and 422 mu M for beta-GIcA-(1 -> 6)-Gal, and those of rNcGlcAase were 38.3 mu M and 378 mu M, respectively. Similar to the native enzyme, rAnGlcAase was able to catalyze the transglycosylation of GlcA residues from PNP beta-GlcA to various monosaccharide acceptors such as Glc, Gal, and Xyl. We propose that both AnGlcAase and NcGlcAase are instances of a novel type of beta-glucuronidase with the capacity to hydrolyze beta-GlcA and 4-Me-beta-GlcA residues of AGPs, although they differ significantly in their preferences. (c) 2008 Elsevier Ltd. All rights reserved.