tert-butyl 2,3-dihydroxy-3-(p-hydroxyphenyl)propionate | 936104-84-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羟基酸及其衍生物
• 英文名称: tert-butyl 2,3-dihydroxy-3-(p-hydroxyphenyl)propionate
• 英文别名: Tert-butyl 2,3-dihydroxy-3-(4-hydroxyphenyl)propanoate；tert-butyl 2,3-dihydroxy-3-(4-hydroxyphenyl)propanoate
• CAS: 936104-84-6
• 化学式: C₁₃H₁₈O₅
• 分子量: 254.283
• InChiKey: ZWXFJUCNGCQKBD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  87
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  tert-butyl 2,3-dihydroxy-3-(p-hydroxyphenyl)propionate 在 sodium hydride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 tert-butyl 2-amino-3-(p-(2-(2-(tert-butoxycarbonylsulfanyl)ethoxy)ethoxy)phenyl)-3-fluoropropionate
  参考文献：
  名称：

  Affinity purification of the key enzyme of nyctinasty controlling the rhythm of leaf movement using gluconamidine ligand

  摘要：

  Synthesis of affinity get aimed for leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG are presented. Gluconamidine-based beta-glucosidase inhibitor was utilized for the ligand of the affinity gel. beta-Glucosidase exhibiting activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited a high substrate specificity toward the leaf-opening factor. (c) 2007 Published by Elsevier Ltd.

  DOI：

  10.1016/j.tetlet.2007.01.085
• 作为产物：
  描述：

  在 sodium methylate 作用下， 以 甲醇 为溶剂， 反应 11.0h， 以13.1 g的产率得到tert-butyl 2,3-dihydroxy-3-(p-hydroxyphenyl)propionate
  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.
• Affinity purification of the key enzyme of nyctinasty controlling the rhythm of leaf movement using gluconamidine ligand
  作者：Eisuke Kato、Takehiko Sasaki、Tadahiro Kumagai、Minoru Ueda

  DOI：10.1016/j.tetlet.2007.01.085

  日期：2007.3

  Synthesis of affinity get aimed for leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG are presented. Gluconamidine-based beta-glucosidase inhibitor was utilized for the ligand of the affinity gel. beta-Glucosidase exhibiting activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited a high substrate specificity toward the leaf-opening factor. (c) 2007 Published by Elsevier Ltd.