tert-butyl 2-azido-3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)-phenyl)-3-hydroxypropionate | 1033617-44-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: tert-butyl 2-azido-3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)-phenyl)-3-hydroxypropionate
• CAS: 1033617-44-5
• 化学式: C₂₂H₃₃N₃O₇S
• 分子量: 483.586
• InChiKey: JDXHQZKZQQWNRU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  33.0
• 可旋转键数：
  11.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  140.05
• 氢给体数：
  1.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  tert-butyl 2-azido-3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)-phenyl)-3-hydroxypropionate 在 4,4'-二氨基二苯乙烯-2,2'-二磺酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.17h， 生成 tert-butyl 2-azido-3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)phenyl)-3-fluoropropionate
  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：

  tert-butyl 3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)-phenyl)-3-hydroxy-2-(p-nitrobenzenesulfonyl)propionate 在 sodium azide 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 15.0h， 以61%的产率得到tert-butyl 2-azido-3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)-phenyl)-3-hydroxypropionate
  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