3,4-dinitrophenyl β-D-xylopyranoside | 71693-33-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3,4-dinitrophenyl β-D-xylopyranoside
• 英文别名: 3,4-Dinitrophenyl beta-D-xylopyranoside；(2S,3R,4S,5R)-2-(3,4-dinitrophenoxy)oxane-3,4,5-triol
• CAS: 71693-33-9
• 化学式: C₁₁H₁₂N₂O₉
• 分子量: 316.224
• InChiKey: AYTNQEKRUAAWSI-YTWAJWBKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.5
• 重原子数：
  22
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  171
• 氢给体数：
  3
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  3,4-dinitrophenyl β-D-xylopyranoside 在 吡啶 、 三氟化硼乙醚 、 水 、 二正丁基氧化锡 、 溶剂黄146 作用下， 以 乙醚 、 二氯甲烷 为溶剂， 反应 3.5h， 生成 3,4-dinitrophenyl 2,3,2',3',4'-penta-O-acetyl-β-D-xylobioside
  参考文献：
  名称：

  Syntheses and testing of substrates and mechanism-based inactivators for xylanases

  摘要：

  The syntheses of the 2,5- and 3,4-dinitrophenyl beta-xylobiosides by two separate routes are described, as well as the syntheses of the 2,4-dinitrophenyl beta-glycosides of 2-chloro-2-deoxyxylobiose and 2-deoxy-2-fluoro-xylobiose. Both the 3,4- and 2,5-dinitrophenyl beta-xylobiosides proved to be good substrates for the Bacillus subtilis xylanase, with k(cat)/K-m values of 1.0 and 34.4 mM(-1) s(-1), respectively. Excellent time-dependent inactivation of the exoxylanase/glucanase from Cellulomonas fimi was provided by 2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-xylobioside,according to inactivation parameters of k(i) = 0.057 min(-1) and K-i = 0.0035 mM.

  DOI：

  10.1016/0008-6215(95)00080-d
• 作为产物：
  描述：

  2,3,4-三-O-乙酰基-α-D-木吡喃糖苷溴 在 2,6-二甲基吡啶 、 sodium methylate 、 silver carbonate 作用下， 以 甲醇 、 乙腈 为溶剂， 生成 3,4-dinitrophenyl β-D-xylopyranoside
  参考文献：
  名称：

  木糖的芳基取代衍生物作为环保型多功能农药的应用

  摘要：

  已经合成了一系列木糖的芳基取代的衍生物。生物学测试表明，所得化合物对各种植物致病真菌具有很高的杀真菌活性。其他生物学研究表明，合成的化合物具有很高的植物生长调节活性。

  DOI：

  10.1134/s1070363216130120

文献信息

• Biochemical identification of the catalytic residues of a glycoside hydrolase family 120 β-xylosidase, involved in xylooligosaccharide metabolisation by gut bacteria
  作者：Davide A. Cecchini、Régis Fauré、Elisabeth Laville、Gabrielle Potocki-Veronese

  DOI：10.1016/j.febslet.2015.08.012

  日期：2015.10.7

  The β‐xylosidase B fromBifidobacterium adolescentis ATCC15703 belongs to the newly characterized family 120 of glycoside hydrolases. In order to investigate its catalytic mechanism, an extensive kinetic study of the wild‐type enzyme and mutants targeting the three highly conserved residues Asp393, Glu416 and Glu364 was performed. NMR analysis of the xyloside hydrolysis products, the change of the reaction rate‐limiting step for the Glu416 mutants, the pH dependency of E416A activity and its chemical rescue allowed to demonstrate that this GH120 enzyme uses a retaining mechanism of glycoside hydrolysis, Glu416 playing the role of acid/base catalyst and Asp393 that of nucleophile.