dimethyl 2-(pyridin-3-ylmethylideneamino)pentanedioate | 928331-25-3

• 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: dimethyl 2-(pyridin-3-ylmethylideneamino)pentanedioate
• CAS: 928331-25-3
• 化学式: C₁₃H₁₆N₂O₄
• 分子量: 264.281
• InChiKey: DNTRABRCOTUNSZ-UHFFFAOYSA-N

物化性质

• 沸点：
  375.0±37.0 °C(Predicted)
• 密度：
  1.15±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.0
• 重原子数：
  19.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  77.85
• 氢给体数：
  0.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  二乙烯基砜 、 dimethyl 2-(pyridin-3-ylmethylideneamino)pentanedioate 在 silver(I) acetate 、 三乙胺 作用下， 以 甲苯 为溶剂， 反应 24.0h， 以72%的产率得到methyl (2SR,4SR,5SR)-4-ethenesulfonyl-2-(2-methoxycarbonylethyl)-5-(pyridin-3-yl)pyrrolidine-2-carboxylate
  参考文献：
  名称：

  Probing of the cis-5-phenyl proline scaffold as a platform for the synthesis of mechanism-based inhibitors of the Staphylococcus aureus sortase SrtA isoform

  摘要：

  cis-5-Phenyl prolinates with electrophilic substituents at the fourth position of a pyrrolidine ring were synthesized by 1,3-dipolar cycloaddition of arylimino esters with divinyl sulfone and acrylonitrile. 4-Vinylsulfonyl 5-phenyl prolinates inhibit Staphylococcus aureus sortase SrtA irreversibly by modification of the enzyme Cys184 and could be used as hits for the development of antibacterials and antivirulence agents. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.02.008
• 作为产物：
  描述：

  3-吡啶甲醛 、 DL-谷氨酸二甲酯盐酸盐 在 magnesium sulfate 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 生成 dimethyl 2-(pyridin-3-ylmethylideneamino)pentanedioate
  参考文献：
  名称：

  Probing of the cis-5-phenyl proline scaffold as a platform for the synthesis of mechanism-based inhibitors of the Staphylococcus aureus sortase SrtA isoform

  摘要：

  cis-5-Phenyl prolinates with electrophilic substituents at the fourth position of a pyrrolidine ring were synthesized by 1,3-dipolar cycloaddition of arylimino esters with divinyl sulfone and acrylonitrile. 4-Vinylsulfonyl 5-phenyl prolinates inhibit Staphylococcus aureus sortase SrtA irreversibly by modification of the enzyme Cys184 and could be used as hits for the development of antibacterials and antivirulence agents. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.02.008