(R)-3-((tert-butyldimethylsilyl)oxy)-1-methoxy-1-oxopropan-2-yl (4E,6E,8E)-6,8-dimethyl-3-oxodeca-4,6,8-trienoate | 1574403-50-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (R)-3-((tert-butyldimethylsilyl)oxy)-1-methoxy-1-oxopropan-2-yl (4E,6E,8E)-6,8-dimethyl-3-oxodeca-4,6,8-trienoate
• CAS: 1574403-50-1
• 化学式: C₂₂H₃₆O₆Si
• 分子量: 424.61
• InChiKey: VPPPTDDIFCTVNT-VKFDSLPHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.52
• 重原子数：
  29.0
• 可旋转键数：
  10.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  78.9
• 氢给体数：
  0.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (R)-3-((tert-butyldimethylsilyl)oxy)-1-methoxy-1-oxopropan-2-yl (4E,6E,8E)-6,8-dimethyl-3-oxodeca-4,6,8-trienoate 在 acyltransferase QmnD₃ 、 四丁基氟化铵 作用下， 以 四氢呋喃 、 aq. phosphate buffer 为溶剂， 反应 3.0h， 生成
  参考文献：
  名称：

  Characterization of QmnD3/QmnD4 for Double Bond Formation in Quartromicin Biosynthesis

  摘要：

  In this work, two enzymes responsible for the biogenesis of possible [4 + 2] reaction precursors in the quartromicin biosynthetic pathway were characterized: acetylation of 1 to yield 2 was catalyzed by QmnD3, and subsequent acetic acid elimination of 2 to form double bond product 3 was catalyzed by QmnD4. Site-directed mutagenesis assay of QmnD3 and QmnD4 was investigated, and a general base-catalyzed mechanism for QmnD4 is proposed.

  DOI：

  10.1021/ol500111n
• 作为产物：
  描述：

  tert-butyl (4E,6E,8E)-6,8-dimethyl-deca-4,6,8-triene-β-ketothionate 、 methyl (2R)-3-(tert-butyldimethylsilyloxy)-2-hydroxypropanoate 在 silver trifluoroacetate 作用下， 以 四氢呋喃 为溶剂， 以86%的产率得到(R)-3-((tert-butyldimethylsilyl)oxy)-1-methoxy-1-oxopropan-2-yl (4E,6E,8E)-6,8-dimethyl-3-oxodeca-4,6,8-trienoate
  参考文献：
  名称：

  Characterization of QmnD3/QmnD4 for Double Bond Formation in Quartromicin Biosynthesis

  摘要：

  In this work, two enzymes responsible for the biogenesis of possible [4 + 2] reaction precursors in the quartromicin biosynthetic pathway were characterized: acetylation of 1 to yield 2 was catalyzed by QmnD3, and subsequent acetic acid elimination of 2 to form double bond product 3 was catalyzed by QmnD4. Site-directed mutagenesis assay of QmnD3 and QmnD4 was investigated, and a general base-catalyzed mechanism for QmnD4 is proposed.

  DOI：

  10.1021/ol500111n