(4-Acetylamino-phenyl)-acetic acid 2-methyl-quinolin-8-yl ester | 118380-00-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: (4-Acetylamino-phenyl)-acetic acid 2-methyl-quinolin-8-yl ester
• 英文别名: 2-Methylquinolin-8-yl (4-acetamidophenyl)acetate；(2-methylquinolin-8-yl) 2-(4-acetamidophenyl)acetate
• CAS: 118380-00-0
• 化学式: C₂₀H₁₈N₂O₃
• 分子量: 334.375
• InChiKey: JGUWBIDVHHPTRS-UHFFFAOYSA-N

物化性质

• 沸点：
  590.2±50.0 °C(Predicted)
• 密度：
  1.264±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  25
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  68.3
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  8-羟基喹哪啶 、 阿克他利 在 双(2-氧代-3-恶唑烷基)次磷酰氯 、 三乙胺 作用下， 生成 (4-Acetylamino-phenyl)-acetic acid 2-methyl-quinolin-8-yl ester
  参考文献：
  名称：

  Substrate attenuation: An approach to improve antibody catalysis

  摘要：

  Antibodies raised to quinaldine phosphonamide 1a showed no ability to hydrolyze its most homologous substrates amide and ester 2 and 3, respectively. However, within this same set of antibodies some thirteen showed a great propensity to hydrolyse a structurally similar naphthyl ester In addition to heteroatom discrimination one of the antibodies examined in detail displayed an increase in catalytic efficiency presumably via weak apparent binding (k(m)) when phenylesters were employed as substrates. These findings suggest abzyme catalysis may be improved via substrate attenuation.

  DOI：

  10.1016/s0040-4020(01)81784-1

文献信息

• Substrate attenuation: An approach to improve antibody catalysis
  作者：Kim D. Janda、Stephen J. Benkovic、Donald A. McLeod、Diane M. Schloeder、Richard A. Lerner

  DOI：10.1016/s0040-4020(01)81784-1

  日期：1991.1

  Antibodies raised to quinaldine phosphonamide 1a showed no ability to hydrolyze its most homologous substrates amide and ester 2 and 3, respectively. However, within this same set of antibodies some thirteen showed a great propensity to hydrolyse a structurally similar naphthyl ester In addition to heteroatom discrimination one of the antibodies examined in detail displayed an increase in catalytic efficiency presumably via weak apparent binding (k(m)) when phenylesters were employed as substrates. These findings suggest abzyme catalysis may be improved via substrate attenuation.