(E)-6-(tert-butyldimethylsilyloxy)hex-2-enyl 2,2,2-trichloroacetimidate | 1240519-07-6

• 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: (E)-6-(tert-butyldimethylsilyloxy)hex-2-enyl 2,2,2-trichloroacetimidate
• 英文别名: (E)-6-(tert-butyldimethylsilyloxy)hex-2-en-1-yl 2,2,2-trichloroacetimidate；[(E)-6-[tert-butyl(dimethyl)silyl]oxyhex-2-enyl] 2,2,2-trichloroethanimidate
• CAS: 1240519-07-6
• 化学式: C₁₄H₂₆Cl₃NO₂Si
• 分子量: 374.81
• InChiKey: GFCJWKJVFSMGNX-WTHPFZPOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.71
• 重原子数：
  21
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  42.3
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (E)-6-(tert-butyldimethylsilyloxy)hex-2-enyl 2,2,2-trichloroacetimidate 在 Hoveyda-Grubbs catalyst second generation 、 [(R)-COP-Cl]2 、 二异丁基氢化铝 、 碳酸氢钠 、 氟化氢吡啶 、 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 、 甲苯 为溶剂， 反应 2.92h， 生成 tert-butyl [ (3S,6R)-6-(3-hydroxypropyl)-2-oxo-3,6-dihydropyridin-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：

  1-(tert-butyldimethylsilyloxy)-4-pentyne 在 正丁基锂 、 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 0.75h， 生成 (E)-6-(tert-butyldimethylsilyloxy)hex-2-enyl 2,2,2-trichloroacetimidate
  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

文献信息

• Catalytic Asymmetric Synthesis of Branched Chiral Allylic Phenyl Ethers from (E)-Allylic Alcohols
  作者：Angela C. Olson、Larry E. Overman、Helen F. Sneddon、Joseph W. Ziller

  DOI：10.1002/adsc.200900678

  日期：2009.12

  family are reported and characterized crystallographically. The di-mu-amidate complex 3 or its enantiomer (ent-3) are the first asymmetric catalysts that allow commercially available, or readily accessible, (E)-2-alkene-1-ols to be transformed to enantioenriched branched allylic aryl ethers upon reaction of their trichloroacetimidate derivatives with phenols. The 3-aryloxy-1-alkene products are formed

  报道了第一个二-mu-酰胺二钯配合物和一种新的 COP（钴恶唑啉钯环）钯 (II) 催化剂家族的二-mu-羧酸二钯配合物，并进行了晶体学表征。二-mu-酰胺配合物 3 或其对映异构体 (ent-3) 是第一个不对称催化剂，它允许市售或容易获得的 (E)-2-烯烃-1-醇转化为对映体富集的支链烯丙基芳基醚它们的三氯乙酰亚胺衍生物与酚类反应。3-芳氧基-1-烯烃产物以高对映体纯度（通常为90-98%ee）和有用产率（61-88%）形成。
• Mechanism-based Inactivation by Aromatization of the Transaminase BioA Involved in Biotin Biosynthesis in <i>Mycobaterium tuberculosis</i>
  作者：Ce Shi、Todd W. Geders、Sae Woong Park、Daniel J. Wilson、Helena I. Boshoff、Orishadipe Abayomi、Clifton E. Barry、Dirk Schnappinger、Barry C. Finzel、Courtney C. Aldrich

  DOI：10.1021/ja204036t

  日期：2011.11.16

  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.