pyranonigrin E

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡喃
• 英文名称: pyranonigrin E
• 英文别名: 3-Hydroxy-6-methyl-7-methylidene-2-nona-1,3-dienylpyrano[2,3-c]pyrrole-4,5-dione；3-hydroxy-6-methyl-7-methylidene-2-nona-1,3-dienylpyrano[2,3-c]pyrrole-4,5-dione
• 化学式: C₁₈H₂₁NO₄
• 分子量: 315.369
• InChiKey: ITJJIMKGOLMIJY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  23
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 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：

  pyranonigrin E 在 nicotinamide adenine dinucleotide phosphate 、 recombinant PynE domain of protein from Aspergillus niger A₁₁₇₉ strain 、 三羟甲基氨基甲烷盐酸盐 、 sodium chloride 作用下， 以 水 为溶剂， 反应 1.0h， 生成 pyranonigrin G
  参考文献：
  名称：

  Elucidation of Pyranonigrin Biosynthetic Pathway Reveals a Mode of Tetramic Acid, Fused γ-Pyrone, and exo-Methylene Formation

  摘要：

  Successful activation of the pyranonigrin biosynthetic gene cluster and gene knockout in Aspergillus niger plus in vivo and in vitro assays led to isolation of six new products, including a spiro cydobutane-containing dimeric compound, which served as the basis for the proposed comprehensive pyranonigrin biosynthetic pathway. Two redox enzymes are key to forming the characteristic fused gamma-pyrone core, and a protease homologue performs the exo-methylene formation.

  DOI：

  10.1021/acs.orglett.5b02435
• 作为产物：
  描述：

  pyranonigrin G 在 Saccharomyces cerevisiae SCKW₁₂ transformed with pKW₂₀₂₂₁ plasmides expressing pynB domain of protein from Aspergillus niger A₁₁₇₉ strain 作用下， 以 水 为溶剂， 反应 4.0h， 生成 pyranonigrin E
  参考文献：
  名称：

  Elucidation of Pyranonigrin Biosynthetic Pathway Reveals a Mode of Tetramic Acid, Fused γ-Pyrone, and exo-Methylene Formation

  摘要：

  Successful activation of the pyranonigrin biosynthetic gene cluster and gene knockout in Aspergillus niger plus in vivo and in vitro assays led to isolation of six new products, including a spiro cydobutane-containing dimeric compound, which served as the basis for the proposed comprehensive pyranonigrin biosynthetic pathway. Two redox enzymes are key to forming the characteristic fused gamma-pyrone core, and a protease homologue performs the exo-methylene formation.

  DOI：

  10.1021/acs.orglett.5b02435