(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

文献信息

• Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results
  作者：Arkadius Pichota、Jeyaraj Duraiswamy、Zheng Yin、Thomas H. Keller、Jenefer Alam、Sarah Liung、Gladys Lee、Mei Ding、Gang Wang、Wai Ling Chan、Mark Schreiber、Ida Ma、David Beer、Xinyi Ngew、Kakoli Mukherjee、Mahesh Nanjundappa、Jeanette W.P. Teo、Pamela Thayalan、Amelia Yap、Thomas Dick、Wuyi Meng、Mei Xu、James Koehn、Shi-Hao Pan、Kirk Clark、Xiaoling Xie、Carolyn Shoen、Michael Cynamon

  DOI：10.1016/j.bmcl.2008.10.040

  日期：2008.12

  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.