N-formylvaline phenyl ester

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-formylvaline phenyl ester
• 英文别名: Phenyl 2-formamido-3-methylbutanoate；phenyl 2-formamido-3-methylbutanoate
• 化学式: C₁₂H₁₅NO₃
• 分子量: 221.256
• InChiKey: XCCKMNMOXGZRAX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  D,L-valine 在 乙酸酐 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 6.0h， 生成 N-formylvaline phenyl ester
  参考文献：
  名称：

  Remote Binding Energy in Antibody Catalysis:  Studies of a Catalytically Unoptimized Specificity Pocket

  摘要：

  Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system, We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes, pie have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes Favorable simultaneous interactions between the side chain and binding packet along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-packet interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (k(cat)) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8,hapten complex has allowed for the identification of differences between the active sites of 17E8; and several proteases, The identified differences give insight to the sources of the inefficient use of binding energy.

  DOI：

  10.1021/ja983017e

文献信息

• Remote Binding Energy in Antibody Catalysis:  Studies of a Catalytically Unoptimized Specificity Pocket
  作者：Herschel Wade、Thomas S. Scanlan

  DOI：10.1021/ja983017e

  日期：1999.2.1

  Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system, We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes, pie have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes Favorable simultaneous interactions between the side chain and binding packet along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-packet interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (k(cat)) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8,hapten complex has allowed for the identification of differences between the active sites of 17E8; and several proteases, The identified differences give insight to the sources of the inefficient use of binding energy.