ethyl 2-(1,4-dihydro-4-oxoquinolin-3-yl)acetate | 959289-76-0

• 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: ethyl 2-(1,4-dihydro-4-oxoquinolin-3-yl)acetate
• 英文别名: Ethyl 4-hydroxy-3-quinolylacetate；ethyl 2-(4-oxo-1H-quinolin-3-yl)acetate
• CAS: 959289-76-0
• 化学式: C₁₃H₁₃NO₃
• 分子量: 231.251
• InChiKey: ZEROWVYODJEUOT-UHFFFAOYSA-N

物化性质

• 沸点：
  360.2±42.0 °C(Predicted)
• 密度：
  1.191±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ethyl 2-(1,4-dihydro-4-oxoquinolin-3-yl)acetate 在 dimethyl sulfide borane 作用下， 以 四氢呋喃 为溶剂， 以59.2%的产率得到3-(2-hydroxyethyl)quinolin-4(1H)-one
  参考文献：
  名称：

  4-Quinolones as Noncovalent Inhibitors of High Molecular Mass Penicillin-Binding Proteins

  摘要：

  Penicillin-binding proteins (PBPs) are important bacterial enzymes that carry out the final steps of bacterial cell wall assembly. Their DD-transpeptidase activity accomplishes the essential peptide cross linking step of the cell wall. To date, all attempts to discover effective inhibitors of PBPs, apart from beta-lactams, have not led to new antibiotics. Therefore, the need for new classes of efficient inhibitors of these enzymes remains. Guided by a computational fragment based docking procedure, carried out on Escherichia cob PBPS, we have designed and synthesized a series of 4-quinolones as potential inhibitors of PBPs. We describe their binding to the PBPs of E cob and Bacillus subtilis. Notably, these compounds bind quite tightly to the essential high molecular mass PBPs.

  DOI：

  10.1021/ml3001006
• 作为产物：
  描述：

  anilinomethylene-succinic acid diethyl ester 在 paraffin oil 作用下， 生成 ethyl 2-(1,4-dihydro-4-oxoquinolin-3-yl)acetate
  参考文献：
  名称：

  DE748540

  摘要：

  公开号：

文献信息

• DE748540
  申请人：——

  公开号：——

  公开（公告）日：——
• 4-Quinolones as Noncovalent Inhibitors of High Molecular Mass Penicillin-Binding Proteins
  作者：Abbas G. Shilabin、Liudmila Dzhekieva、Pushpa Misra、B. Jayaram、R. F. Pratt

  DOI：10.1021/ml3001006

  日期：2012.7.12

  Penicillin-binding proteins (PBPs) are important bacterial enzymes that carry out the final steps of bacterial cell wall assembly. Their DD-transpeptidase activity accomplishes the essential peptide cross linking step of the cell wall. To date, all attempts to discover effective inhibitors of PBPs, apart from beta-lactams, have not led to new antibiotics. Therefore, the need for new classes of efficient inhibitors of these enzymes remains. Guided by a computational fragment based docking procedure, carried out on Escherichia cob PBPS, we have designed and synthesized a series of 4-quinolones as potential inhibitors of PBPs. We describe their binding to the PBPs of E cob and Bacillus subtilis. Notably, these compounds bind quite tightly to the essential high molecular mass PBPs.