4-氯-6-(4-硝基-苯基)-嘧啶-2-基胺 | 100911-98-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 中文名称: 4-氯-6-(4-硝基-苯基)-嘧啶-2-基胺
• 英文名称: 4-Chloro-6-(4-nitro-phenyl)-pyrimidin-2-ylamine
• CAS: 100911-98-6
• 化学式: C₁₀H₇ClN₄O₂
• 分子量: 250.644
• InChiKey: LMJQHRLVGJXDBV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.29
• 重原子数：
  17.0
• 可旋转键数：
  2.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  94.94
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  4-氯-6-(4-硝基-苯基)-嘧啶-2-基胺 在 Pd-BaSO₄ 氢气 、 sodium cyanoborohydride 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 、 溶剂黄146 、 正丁醇 为溶剂， 反应 18.33h， 生成 2-(3-{4-[2-Amino-6-(indan-2-ylamino)-pyrimidin-4-yl]-phenylamino}-propyl)-phenol
  参考文献：
  名称：

  Novel Inhibitors of Erm Methyltransferases from NMR and Parallel Synthesis

  摘要：

  The Erm family of methyltransferases confers resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics through the methylation of 23S ribosomal RNA. Upon the methylation of RNA, the MLS antibiotics lose their ability to bind to the ribosome and exhibit their antibiotic activity. Using an NMR-based screen, we identified a series of triazine-containing compounds that bind weakly to ErmAM. These initial lead compounds were optimized by the parallel synthesis of a large number of analogues, resulting in compounds which inhibit the Erm-mediated methylation of rRNA in the low micromolar range. NMR and X-ray structures of enzyme/inhibitor complexes reveal that the inhibitors bind to the S-adenosylmethionine binding site on the Erm protein. These compounds represent novel methyltransferase inhibitors that serve as new leads for the reversal of Erm-mediated MLS antibiotic resistance.

  DOI：

  10.1021/jm990293a
• 作为产物：
  描述：

  2-amino-1,6-dihydro-4-(4'-nitrophenyl)-6-oxopyrimidine 在 三氯氧磷 作用下， 反应 3.0h， 生成 4-氯-6-(4-硝基-苯基)-嘧啶-2-基胺
  参考文献：
  名称：

  Novel Inhibitors of Erm Methyltransferases from NMR and Parallel Synthesis

  摘要：

  The Erm family of methyltransferases confers resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics through the methylation of 23S ribosomal RNA. Upon the methylation of RNA, the MLS antibiotics lose their ability to bind to the ribosome and exhibit their antibiotic activity. Using an NMR-based screen, we identified a series of triazine-containing compounds that bind weakly to ErmAM. These initial lead compounds were optimized by the parallel synthesis of a large number of analogues, resulting in compounds which inhibit the Erm-mediated methylation of rRNA in the low micromolar range. NMR and X-ray structures of enzyme/inhibitor complexes reveal that the inhibitors bind to the S-adenosylmethionine binding site on the Erm protein. These compounds represent novel methyltransferase inhibitors that serve as new leads for the reversal of Erm-mediated MLS antibiotic resistance.

  DOI：

  10.1021/jm990293a