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tert-butyl trans-p-O-acetyl coumarate | 1033617-34-3

中文名称
——
中文别名
——
英文名称
tert-butyl trans-p-O-acetyl coumarate
英文别名
——
tert-butyl trans-p-O-acetyl coumarate化学式
CAS
1033617-34-3
化学式
C15H18O4
mdl
——
分子量
262.306
InChiKey
VUKBMWXTRSFLBX-JXMROGBWSA-N
BEILSTEIN
——
EINECS
——
  • 物化性质
  • 计算性质
  • ADMET
  • 安全信息
  • SDS
  • 制备方法与用途
  • 上下游信息
  • 反应信息
  • 文献信息
  • 表征谱图
  • 同类化合物
  • 相关功能分类
  • 相关结构分类

计算性质

  • 辛醇/水分配系数(LogP):
    2.97
  • 重原子数:
    19.0
  • 可旋转键数:
    3.0
  • 环数:
    1.0
  • sp3杂化的碳原子比例:
    0.33
  • 拓扑面积:
    52.6
  • 氢给体数:
    0.0
  • 氢受体数:
    4.0

上下游信息

  • 上游原料
    中文名称 英文名称 CAS号 化学式 分子量

反应信息

  • 作为反应物:
    描述:
    tert-butyl trans-p-O-acetyl coumarate四氧化锇N-甲基吗啉氧化物 作用下, 以 乙腈叔丁醇 为溶剂, 反应 18.0h, 生成
    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:
    叔丁基三氯乙酰亚胺酯反式-4-乙酰氧基肉桂酸三氟化硼乙醚 作用下, 以 四氢呋喃 为溶剂, 反应 0.5h, 以6.01 g的产率得到tert-butyl trans-p-O-acetyl coumarate
    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
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