[S-(E)]-α-[[3-(4-chlorophenyl)-1-oxo-2-propenyl]oxy]benzenepropanoic acid | 61556-61-4

• 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: [S-(E)]-α-[[3-(4-chlorophenyl)-1-oxo-2-propenyl]oxy]benzenepropanoic acid
• 英文别名: -α-<<3-(4-chlorophenyl)-1-oxo-2-propenyl>oxy>benzenepropanoic acid；O-(trans-p-chlorocinnamoyl)-L-β-phenyllactic acid；O-(trans-p-chlorocinnamoyl)-L-phenyllactic acid
• CAS: 61556-61-4
• 化学式: C₁₈H₁₅ClO₄
• 分子量: 330.768
• InChiKey: BICQQWGOUWCASB-KXKDPZRNSA-N

物化性质

• 沸点：
  523.2±50.0 °C(Predicted)
• 密度：
  1.317±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.59
• 重原子数：
  23.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  63.6
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  [S-(E)]-α-[[3-(4-chlorophenyl)-1-oxo-2-propenyl]oxy]benzenepropanoic acid 在 carboxypeptidase A 作用下， 以 水 为溶剂， 生成 对氯肉桂酸 、 L-(-)-3-苯基乳酸
  参考文献：
  名称：

  Carboxypeptidase A-catalyzed hydrolysis of .alpha.-(acylamino)cinnamoyl derivatives of L-.beta.-phenyllactate and L-phenylalaninate: evidence for acyl-enzyme intermediates

  摘要：

  DOI：

  10.1021/ja00301a025

文献信息

• Catalytic Hydrolysis of Acylcyanamide Substrates by Carboxypeptidase A Defines the Stereochemistry of Carbonyl Hydration at the Enzyme Active Site
  作者：W.L. Mock、X.D. Xu

  DOI：10.1006/bioo.1994.1031

  日期：1994.12

  New peptide and ester substrate analogues for carboxypeptidase A have been prepared which differ by the possession of an acylcyanamide residue of comparable acidity in place of the C-terminal carboxylic acid group that is normally required by the enzyme. The surrogates are cleaved respectively 2 x 10(5) and 10(4) times more slowly than corresponding regular substrates (k(cat)/K-m). The suggested interpretation is that the carboxylate functionality of normal substrates, in addition to conferring specificity, participates in the enzymic reaction mechanism as a general base, and that this becomes disallowed in the new analogues by specific-binding interactions which induce the cyano substituent to interfere with hydration of the scissile linkage. That reasoning controverts widely accepted ideas regarding the stereochemical course of H2O addition to the enzymic Zn2+-activated peptide linkage as well as the role of carboxypeptidase active site residue Glu 270 in the catalytic mechanism. (C) 1994 Academic Press, Inc.
• Carboxypeptidase A-catalyzed hydrolysis of .alpha.-(acylamino)cinnamoyl derivatives of L-.beta.-phenyllactate and L-phenylalaninate: evidence for acyl-enzyme intermediates
  作者：Junghun Suh、Wonhwa Cho、Shin Chung

  DOI：10.1021/ja00301a025

  日期：1985.7