ethyl (Z)-p-(diethylamino)-o-methoxy-α-methylcinnamate | 151775-14-3

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: ethyl (Z)-p-(diethylamino)-o-methoxy-α-methylcinnamate
• CAS: 151775-14-3
• 化学式: C₁₇H₂₅NO₃
• 分子量: 291.39
• InChiKey: XTMSFAWFOIWXDN-QBFSEMIESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.51
• 重原子数：
  21.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  38.77
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  ethyl (Z)-p-(diethylamino)-o-methoxy-α-methylcinnamate 以 various solvent(s) 为溶剂， 生成 ethyl (E)-p-(diethylamino)-o-methoxy-α-methylcinnamate
  参考文献：
  名称：

  Photochemistry of enzyme-bound cinnamoyl derivatives

  摘要：

  p-(Diethylamino)-o-hydroxy-alpha-methylcinnamoyl (CINN) was used as an acylating moiety for the formation of stable CINN-enzymes at the active site serine residues of the enzymes chymotrypsin, Factor Xa, and thrombin. Photolysis of the stable CINN-enzymes generates enzymatic activity via the proposed consecutive steps of photoisomerization (rate-determining step) and thermal lactonization (fast). Photochemical studies were undertaken to assess how an enzyme active site could alter the photochemistry of the cinnamoyl derivative. Quantum yields for E to Z photoisomerization (PHI(E-->Z)) were measured for the three CINN-enzymes at 366 nm (20-degrees-C in pH 7.4 Tris buffer) and for the model system ethyl p-(diethylamino)-o-hydroxy-alpha-methylcinnamate (CINN-OEt). Relative to the value of PHI(E-->Z) = 0.13 for CINN-OEt, CINN actually displayed an enhanced isomerization efficiency while bound at the active sites of chymotrypsin and Factor Xa (PHI(E-->Z) = 0.17 and 0.23, respectively) and a decreased isomerization efficiency (PHI(E-->Z) = 0.04) while bound to thrombin. The influence of chymotrypsin's active site on cinnamoyl photoisomerization was investigated further by measuring the photostationary state isomeric ratios for MeCINN-chymotrypsin and MeCINN-OEt, the methyl ether analogue of the corresponding CINN photolytes, in pH 7.4 Tris buffer. MeCINN-chymotrypsin displayed a value of 2.7 for PHI(Z-->E)/(PHI(E-->Z = quantum yield for E to Z and PHI(Z-->E) = quantum yield for Z to E), and MeCINN-OEt exhibited a value of 1.7. This difference could not be attributed to the greater hydrophobicity of chymotrypsin's active site since values of PHI(Z-->E/PHI(E-->Z) for MeCINN-OEt in organic solvents were less than unity. Photoisomerization quantum yields were also measured for the isomers of MeCINN-chymotrypsin and MeCINN-OEt. Both acyl-enzyme isomers exhibited less efficient photoisomerization (E to Z and Z to E) than their respective model system, MeCINN-OEt.

  DOI：

  10.1021/ja00074a002
• 作为产物：
  描述：

  ethyl (E)-p-(diethylamino)-o-hydroxy-α-methylcinnamate 在 sodium hydride 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.33h， 生成 ethyl (Z)-p-(diethylamino)-o-methoxy-α-methylcinnamate
  参考文献：
  名称：

  Photochemistry of enzyme-bound cinnamoyl derivatives

  摘要：

  p-(Diethylamino)-o-hydroxy-alpha-methylcinnamoyl (CINN) was used as an acylating moiety for the formation of stable CINN-enzymes at the active site serine residues of the enzymes chymotrypsin, Factor Xa, and thrombin. Photolysis of the stable CINN-enzymes generates enzymatic activity via the proposed consecutive steps of photoisomerization (rate-determining step) and thermal lactonization (fast). Photochemical studies were undertaken to assess how an enzyme active site could alter the photochemistry of the cinnamoyl derivative. Quantum yields for E to Z photoisomerization (PHI(E-->Z)) were measured for the three CINN-enzymes at 366 nm (20-degrees-C in pH 7.4 Tris buffer) and for the model system ethyl p-(diethylamino)-o-hydroxy-alpha-methylcinnamate (CINN-OEt). Relative to the value of PHI(E-->Z) = 0.13 for CINN-OEt, CINN actually displayed an enhanced isomerization efficiency while bound at the active sites of chymotrypsin and Factor Xa (PHI(E-->Z) = 0.17 and 0.23, respectively) and a decreased isomerization efficiency (PHI(E-->Z) = 0.04) while bound to thrombin. The influence of chymotrypsin's active site on cinnamoyl photoisomerization was investigated further by measuring the photostationary state isomeric ratios for MeCINN-chymotrypsin and MeCINN-OEt, the methyl ether analogue of the corresponding CINN photolytes, in pH 7.4 Tris buffer. MeCINN-chymotrypsin displayed a value of 2.7 for PHI(Z-->E)/(PHI(E-->Z = quantum yield for E to Z and PHI(Z-->E) = quantum yield for Z to E), and MeCINN-OEt exhibited a value of 1.7. This difference could not be attributed to the greater hydrophobicity of chymotrypsin's active site since values of PHI(Z-->E/PHI(E-->Z) for MeCINN-OEt in organic solvents were less than unity. Photoisomerization quantum yields were also measured for the isomers of MeCINN-chymotrypsin and MeCINN-OEt. Both acyl-enzyme isomers exhibited less efficient photoisomerization (E to Z and Z to E) than their respective model system, MeCINN-OEt.

  DOI：

  10.1021/ja00074a002