ethyl-3-(2-(phenylamino)pyrimidin-4-ylamino)benzoate | 1595282-69-1

• 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: ethyl-3-(2-(phenylamino)pyrimidin-4-ylamino)benzoate
• CAS: 1595282-69-1
• 化学式: C₁₉H₁₈N₄O₂
• 分子量: 334.378
• InChiKey: WWAUAIBCWFVZEC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.14
• 重原子数：
  25.0
• 可旋转键数：
  6.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  76.14
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  ethyl-3-(2-(phenylamino)pyrimidin-4-ylamino)benzoate 在 四溴化碳 、 水 、 二异丁基氢化铝 、 三苯基膦 、 sodium hydroxide 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 、 甲苯 为溶剂， 反应 14.08h， 生成 (S)-4-(3-(2-(phenylamino)pyrimidin-4-ylamino)benzylthio)-2-aminobutanoic acid trifluoroacetate
  参考文献：
  名称：

  Using ‘biased-privileged’ scaffolds to identify lysine methyltransferase inhibitors

  摘要：

  Methylation of histones by lysine methyltransferases (KMTases) plays important roles in regulating chromatin function. It is also now clear that improper KMTases activity is linked to human diseases, such as cancer. We report an approach that employs drug-like 'privileged' scaffolds biased with motifs present in S-adenosyl methionine, the cofactor used by KMTases, to efficiently generate inhibitors for Set7, a biochemically well-characterized KMTase. Setin-1, the most potent inhibitor of Set7 we have developed also inhibits the KMTase G9a. Together these data suggest that these inhibitors should provide good starting points to generate useful probes for KMTase biology and guide the design of KMTase inhibitors with drug-like properties. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.02.024
• 作为产物：
  描述：

  3-氨基苯甲酸乙酯 、 2,4-二氯嘧啶 、 苯胺 在 二异丙胺 、 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 17.0h， 生成 ethyl-3-(2-(phenylamino)pyrimidin-4-ylamino)benzoate
  参考文献：
  名称：

  Using ‘biased-privileged’ scaffolds to identify lysine methyltransferase inhibitors

  摘要：

  Methylation of histones by lysine methyltransferases (KMTases) plays important roles in regulating chromatin function. It is also now clear that improper KMTases activity is linked to human diseases, such as cancer. We report an approach that employs drug-like 'privileged' scaffolds biased with motifs present in S-adenosyl methionine, the cofactor used by KMTases, to efficiently generate inhibitors for Set7, a biochemically well-characterized KMTase. Setin-1, the most potent inhibitor of Set7 we have developed also inhibits the KMTase G9a. Together these data suggest that these inhibitors should provide good starting points to generate useful probes for KMTase biology and guide the design of KMTase inhibitors with drug-like properties. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.02.024