Tert-butyl 2-amino-3-[4-[tert-butyl(dimethyl)silyl]oxyphenyl]-3-fluoropropanoate | 960316-84-1

• 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-amino-3-[4-[tert-butyl(dimethyl)silyl]oxyphenyl]-3-fluoropropanoate
• CAS: 960316-84-1
• 化学式: C₁₉H₃₂FNO₃Si
• 分子量: 369.552
• InChiKey: VBSURLPCWPATJV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.75
• 重原子数：
  25
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  61.6
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Tert-butyl 2-amino-3-[4-[tert-butyl(dimethyl)silyl]oxyphenyl]-3-fluoropropanoate 、 D-gluconothionolactam 在 N-溴代丁二酰亚胺(NBS) 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 以13.9 mg的产率得到tert-butyl (Z)-2-(N,N-glucoamidine)-3-(p-hydroxyphenyl)acrylate
  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 2-azido-3-(p-(tert-butyldimethylsilyloxy)phenyl)-3-fluoropropionate 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 为溶剂， 反应 12.0h， 生成 Tert-butyl 2-amino-3-[4-[tert-butyl(dimethyl)silyl]oxyphenyl]-3-fluoropropanoate
  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

文献信息

• Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L
  作者：Eisuke Kato、Takehiko Sasaki、Minoru Ueda

  DOI：10.1016/j.bmc.2008.02.035

  日期：2008.4

  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.