ethyl (E)-p-(diethylamino)-o-methoxy-α-methylcinnamate | 151775-11-0

• 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 (E)-p-(diethylamino)-o-methoxy-α-methylcinnamate
• 英文别名: ethyl (E)-3-[4-(diethylamino)-2-methoxyphenyl]-2-methylprop-2-enoate
• CAS: 151775-11-0
• 化学式: C₁₇H₂₅NO₃
• 分子量: 291.39
• InChiKey: XTMSFAWFOIWXDN-ACCUITESSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  21
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  38.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ethyl (E)-p-(diethylamino)-o-methoxy-α-methylcinnamate 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 2.0h， 以91%的产率得到(E)-p-(diethylamino)-o-methoxy-α-methylcinnamic acid
  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 (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

文献信息

• LIGHT ACTIVATED ACYL-ENZYMES
  申请人：DUKE UNIVERSITY

  公开号：EP0489836A1

  公开（公告）日：1992-06-17
• EP0489836A4
  申请人：——

  公开号：EP0489836A4

  公开（公告）日：1993-05-26
• US5114851A
  申请人：——

  公开号：US5114851A

  公开（公告）日：1992-05-19
• US5218137A
  申请人：——

  公开号：US5218137A

  公开（公告）日：1993-06-08
• [EN] LIGHT ACTIVATED ACYL-ENZYMES
  申请人：DUKE UNIVERSITY

  公开号：WO1991003549A1

  公开（公告）日：1991-03-21

  (EN) Light activated acyl-enzymes of formula (III) are disclosed. In the compounds of formula (III) ENZ is an enzyme, X is O or S, Y is -NR3R4, -OR5, or -SR5, and Z is a nucleophile; m is 0 to 3 and n is 1 or 2; Y is substituted on the ring at either or both of the 4 and 6 position. R1 and R2 are each independently H, C1 to C4 alkyl, C3 to C4 unconjugated alkenyl, or C3 to C4 unconjugated alkynyl. R3 and R4 are each independently H, C1 to C4 alkyl, C3 to C4 unconjugated alkenyl, or C3 to C4 unconjugated alkynyl, except that R3 and R4 are not simultaneously both H. R5 is C1 to C4 alkyl, C3 to C4 unconjugated alkenyl, or C3 to C4 unconjugated alkynyl. Methods of using the acyl-enzymes and intermediates for making the acyl-enzymes are disclosed. A preferred intermediate is 2-propenoic acid, 3-(2-hydroxy-4-diethylaminophenyl)-2-methyl-, 4-(aminoiminomethyl)phenyl ester, (E)-, monohydrochloride salt, which is preferably reacted with thrombin to form an acyl-thrombin.(FR) Des enzymes-acyls activés par la lumière de la formule (III) sont divulgués. Dans les composés de la formule (III), ENZ est un enzyme, X est O ou S, Y est -NR3R4, -OR5, ou -SR5, et Z est un nucléophile; m est 0 à 3 et n est 1 ou 2. Y est substitué dans l'anneau soit à l'une soit à l'autre des positions 4 et 6, soit aux deux positions. R1 et R2 sont chacun indépendamment H, alkyle C1 à C4, alkényle non conjugué de C3 à C4, ou alkynyle non conjugué de C3 à C4, sauf que R3 et R4 ne sont pas simultanément H. R5 est alkyle de C1 à C4, alkényle non conjugué de C3 à C4, ou alkynyle non conjugué de C3 à C4. On décrit des procédés pour l'utilisation des enzymes-acyls et les intermédiaires. Un intermédiaire préféré est acide-propénoïque-2, phényle-ester 3-(2-hydroxy-4-diéthylaminophényle)-2-méthyle, 4-(aminoiminométhyle), (E)-, sel monohydrochlorure, que l'on fait réagir, préférablement, avec de la thrombine de manière à produire une thrombine-acyl.