(2R)-2-(cyclopropylmethyl)-3-[formyl(phenylmethoxy)amino]propanoic acid | 1104950-95-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (2R)-2-(cyclopropylmethyl)-3-[formyl(phenylmethoxy)amino]propanoic acid
• CAS: 1104950-95-9
• 化学式: C₁₅H₁₉NO₄
• 分子量: 277.32
• InChiKey: MJBPKAQMAKYDBO-CQSZACIVSA-N

物化性质

• 沸点：
  443.3±55.0 °C(Predicted)
• 密度：
  1.240±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  20
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  66.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2R)-2-(cyclopropylmethyl)-3-[formyl(phenylmethoxy)amino]propanoic acid 、 (S)-2-pyrrolidin-2-yl-1H-benzoimidazole 在 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成
  参考文献：
  名称：

  Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results

  摘要：

  Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.

  DOI：

  10.1016/j.bmcl.2008.10.040
• 作为产物：
  描述：

  甲酸 、 在 乙酸酐 作用下， 生成 (2R)-2-(cyclopropylmethyl)-3-[formyl(phenylmethoxy)amino]propanoic acid
  参考文献：
  名称：

  Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results

  摘要：

  Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.

  DOI：

  10.1016/j.bmcl.2008.10.040