(R)-3-(nitroso)-N-(1-phenylethyl)-5-(trifluoromethyl)benzamide | 1247019-16-4

• 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: (R)-3-(nitroso)-N-(1-phenylethyl)-5-(trifluoromethyl)benzamide
• 英文别名: 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide
• CAS: 1247019-16-4
• 化学式: C₁₆H₁₃F₃N₂O₂
• 分子量: 322.287
• InChiKey: BSSIQTMZYBAPMT-SNVBAGLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  23
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  58.5
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  谷胱甘肽 、 (R)-3-(nitroso)-N-(1-phenylethyl)-5-(trifluoromethyl)benzamide 以 MeOD 、 water-d2 为溶剂， 反应 0.08h， 生成 (S)-2-amino-5-((R)-1-(1-carboxymethylamino)-3-(hydroxy(3-((R)-1-phenylethylcarbamoyl)-5-(trifluoromethyl)phenyl)aminothio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid
  参考文献：
  名称：

  Benzothiazinones: Prodrugs That Covalently Modify the Decaprenylphosphoryl-β-d-ribose 2′-epimerase DprE1 of Mycobacterium tuberculosis

  摘要：

  Benzothiazinones (BTZs) form a new class of potent antimycobacterial agents. Although the target of BTZs has been identified as decaprenylphosphoryl-beta-D-ribose 2'-epimerase (DprE1), their detailed mechanism of action remains obscure. Here we demonstrate that BTZs are activated in the bacterium by reduction of an essential nitro group to a nitroso derivative, which then specifically reacts with a cysteine residue in the active site of DprE1.

  DOI：

  10.1021/ja106357w
• 作为产物：
  描述：

  (R)-3-nitro-N-(1-phenylethyl)-5-(trifluoromethyl)benzamide 在 双氧水 作用下， 以 环己烷 、 叔丁醇 为溶剂， 以65%的产率得到(R)-3-(nitroso)-N-(1-phenylethyl)-5-(trifluoromethyl)benzamide
  参考文献：
  名称：

  Benzothiazinones: Prodrugs That Covalently Modify the Decaprenylphosphoryl-β-d-ribose 2′-epimerase DprE1 of Mycobacterium tuberculosis

  摘要：

  Benzothiazinones (BTZs) form a new class of potent antimycobacterial agents. Although the target of BTZs has been identified as decaprenylphosphoryl-beta-D-ribose 2'-epimerase (DprE1), their detailed mechanism of action remains obscure. Here we demonstrate that BTZs are activated in the bacterium by reduction of an essential nitro group to a nitroso derivative, which then specifically reacts with a cysteine residue in the active site of DprE1.

  DOI：

  10.1021/ja106357w