p-(2-叠氮乙氧基乙氧基)-N-(2-苄氧基硫代乙酰基)苯胺 | 1033617-48-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 中文名称: p-(2-叠氮乙氧基乙氧基)-N-(2-苄氧基硫代乙酰基)苯胺
• 英文名称: p-(2-azidoethoxyethoxy)-N-(2-benzyloxythioacetyl)aniline
• CAS: 1033617-48-9
• 化学式: C₁₉H₂₂N₄O₃S
• 分子量: 386.475
• InChiKey: MBELPLZMXQKKDE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.35
• 重原子数：
  27.0
• 可旋转键数：
  12.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  88.48
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  2,3,4,6-tetra-O-acetyl-D-glucosyl-1-amine 、 p-(2-叠氮乙氧基乙氧基)-N-(2-苄氧基硫代乙酰基)苯胺 在 trimethoxonium tetrafluoroborate 、 4 A molecular sieve 、 N-溴代丁二酰亚胺(NBS) 作用下， 以 二氯甲烷 为溶剂， 反应 2.42h， 以56%的产率得到N-(p-(2-azidoethoxyethoxy)phenyl)-N'-(2,3,4,6-tetraacetyl-1-β-D-glucopyranosyl)benzyloxymethylamidine
  参考文献：
  名称：

  Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L

  摘要：

  The synthesis of an affinity gel aimed at leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG is presented. A gluconamidine-based beta-glucosidase inhibitor was used as the ligand of the affinity gel. beta-Glucosidase exhibiting an activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited high substrate specificity toward the leaf-opening factor. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.02.035
• 作为产物：
  描述：

  p-(2-azidoethoxyethoxy)-N-(2-benzyloxyacetyl)aniline 在 劳森试剂 作用下， 以 甲苯 为溶剂， 反应 1.0h， 以58%的产率得到p-(2-叠氮乙氧基乙氧基)-N-(2-苄氧基硫代乙酰基)苯胺
  参考文献：
  名称：

  Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L

  摘要：

  The synthesis of an affinity gel aimed at leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG is presented. A gluconamidine-based beta-glucosidase inhibitor was used as the ligand of the affinity gel. beta-Glucosidase exhibiting an activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited high substrate specificity toward the leaf-opening factor. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.02.035