benzyl 2-benzyl-2-methylbut-3-enoate | 428510-43-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: benzyl 2-benzyl-2-methylbut-3-enoate
• CAS: 428510-43-4
• 化学式: C₁₉H₂₀O₂
• 分子量: 280.367
• InChiKey: YUZNWCVQICLANZ-UHFFFAOYSA-N

反应信息

• 作为反应物：
  描述：

  benzyl 2-benzyl-2-methylbut-3-enoate 在 palladium on activated charcoal dipotassium hydrogenphosphate 、 氢气 、 间氯过氧苯甲酸 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 52.0h， 生成 erythro-(+/-)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
  参考文献：
  名称：

  Syntheses and Kinetic Evaluation of Racemic and Optically Active 2-Benzyl-2-methyl-3,4-epoxybutanoic Acids as Irreversible Inactivators for Carboxypeptidase A

  摘要：

  Racemic and optically active 2-benzyl-2-methyl-3,4-epoxybutanoic acids were synthesized and evaluated as inactivators for carboxypeptidase A. a representative zinc-containing proteolytic enzyme. Only the threo-form of the inactivator is effective and its potency in terms of k(inact)/K-I value is lower by 42-fold compared with 2-benzyl-3,4-epoxybutanoic acid, indicating that the alpha-methyl group affects adversely in the inactivation contrary to the expectation that it would enhance the inactivation activity of the inhibitor through additional interactions of the methyl group with a small cavity (alpha-methyl hole) present next to the S-1' hydrophobic pocket. Of the enantiomeric pair, the inactivator having the (2S,3R)-configuration is more potent than its enantiomer by 44-fold. The observed kinetic results may be rationalized on the basis that the methyl group in the inactivator having the (2R,3S)configuration experiences the van der Waals repulsive interactions with the bottom of the active site crevice in binding to CPA, casting a doubt on the presence of the so-called alpha-methyl hole at the active site of carboxypeptidase A. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(01)00340-6
• 作为产物：
  描述：

  溴甲苯 、 benzyl 2-benzyl-2-methylbut-3-enoate 以 N,N-二甲基甲酰胺 为溶剂， 以0.65 g的产率得到benzyl 2-benzyl-2-methylbut-3-enoate
  参考文献：
  名称：

  Syntheses and Kinetic Evaluation of Racemic and Optically Active 2-Benzyl-2-methyl-3,4-epoxybutanoic Acids as Irreversible Inactivators for Carboxypeptidase A

  摘要：

  Racemic and optically active 2-benzyl-2-methyl-3,4-epoxybutanoic acids were synthesized and evaluated as inactivators for carboxypeptidase A. a representative zinc-containing proteolytic enzyme. Only the threo-form of the inactivator is effective and its potency in terms of k(inact)/K-I value is lower by 42-fold compared with 2-benzyl-3,4-epoxybutanoic acid, indicating that the alpha-methyl group affects adversely in the inactivation contrary to the expectation that it would enhance the inactivation activity of the inhibitor through additional interactions of the methyl group with a small cavity (alpha-methyl hole) present next to the S-1' hydrophobic pocket. Of the enantiomeric pair, the inactivator having the (2S,3R)-configuration is more potent than its enantiomer by 44-fold. The observed kinetic results may be rationalized on the basis that the methyl group in the inactivator having the (2R,3S)configuration experiences the van der Waals repulsive interactions with the bottom of the active site crevice in binding to CPA, casting a doubt on the presence of the so-called alpha-methyl hole at the active site of carboxypeptidase A. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(01)00340-6