(S)-6-(tert-butyldimethylsilyloxy)hex-1-en-3-amine | 1345841-41-9

• 分子结构分类: 有机化合物 - 有机金属化合物 - 有机类金属化合物
• 英文名称: (S)-6-(tert-butyldimethylsilyloxy)hex-1-en-3-amine
• 英文别名: (3S)-6-[tert-butyl(dimethyl)silyl]oxyhex-1-en-3-amine
• CAS: 1345841-41-9
• 化学式: C₁₂H₂₇NOSi
• 分子量: 229.438
• InChiKey: CABSEJWUERTNEV-LLVKDONJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  15
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  35.2
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (S)-6-(tert-butyldimethylsilyloxy)hex-1-en-3-amine 在 Hoveyda-Grubbs catalyst second generation 、 碳酸氢钠 、 3-(二乙氧基邻酰氧基)-1,2,3-苯并三嗪-4-酮 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 生成 tert-butyl {(3R,6S)-6-[3-(tert-butyldimethylsilyloxy)propyl]-2-oxo-3,6-dihydro-pyridin-3-yl}carbamate
  参考文献：
  名称：

  Mechanism-based Inactivation by Aromatization of the Transaminase BioA Involved in Biotin Biosynthesis in Mycobaterium tuberculosis

  摘要：

  BioA catalyzes the second step of biotin biosynthesis, and this enzyme represents a potential target to develop new antitubercular agents. Herein we report the design, synthesis, and biochemical characterization of a mechanism-based inhibitor (1) featuring a 3,6-dihydropyrid-2-one heterocycle that covalently modifies the pyridoxal S'-phosphate (PLP) cofactor of BioA through aromatization. The structure of the PLP adduct was confirmed by MS/MS and X-ray crystallography at 1.94 angstrom resolution. Inactivation of BioA by 1 was time- and concentration-dependent and protected by substrate. We used a conditional knock-down mutant of M. tuberculosis to demonstrate the antitubercular activity of 1 correlated with BioA expression, and these results provide support for the designed mechanism of action.

  DOI：

  10.1021/ja204036t
• 作为产物：
  描述：

  叔丁基二甲基氯硅烷 在 咪唑 、 正丁基锂 、 [(S)-COP-Cl]2 、 二异丁基氢化铝 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 红铝 作用下， 以 四氢呋喃 、 乙醚 、 正己烷 、 二氯甲烷 、 甲苯 为溶剂， 反应 4.5h， 生成 (S)-6-(tert-butyldimethylsilyloxy)hex-1-en-3-amine
  参考文献：
  名称：

  Mechanism-based Inactivation by Aromatization of the Transaminase BioA Involved in Biotin Biosynthesis in Mycobaterium tuberculosis

  摘要：

  BioA catalyzes the second step of biotin biosynthesis, and this enzyme represents a potential target to develop new antitubercular agents. Herein we report the design, synthesis, and biochemical characterization of a mechanism-based inhibitor (1) featuring a 3,6-dihydropyrid-2-one heterocycle that covalently modifies the pyridoxal S'-phosphate (PLP) cofactor of BioA through aromatization. The structure of the PLP adduct was confirmed by MS/MS and X-ray crystallography at 1.94 angstrom resolution. Inactivation of BioA by 1 was time- and concentration-dependent and protected by substrate. We used a conditional knock-down mutant of M. tuberculosis to demonstrate the antitubercular activity of 1 correlated with BioA expression, and these results provide support for the designed mechanism of action.

  DOI：

  10.1021/ja204036t