6,8-dihydroxy-3-(2-oxopropyl)-1H-isochromen-1-one | 256432-28-7

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 异香豆素及其衍生物
• 英文名称: 6,8-dihydroxy-3-(2-oxopropyl)-1H-isochromen-1-one
• 英文别名: 3-(2-Oxopropyl)-6,8-dihydroxyisocoumarin；6,8-dihydroxy-3-(2-oxopropyl)isochromen-1-one
• CAS: 256432-28-7
• 化学式: C₁₂H₁₀O₅
• 分子量: 234.208
• InChiKey: ASXQQFFJWJUYLO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  17
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  83.8
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  2,4-二羟基-6-甲基甲酸乙酯 在 四甲基乙二胺 、 四丁基碘化铵 、 N,N-二异丙基乙胺 、 lithium hexamethyldisilazane 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 生成 6,8-dihydroxy-3-(2-oxopropyl)-1H-isochromen-1-one
  参考文献：
  名称：

  Characterization of a Fungal Thioesterase Having Claisen Cyclase and Deacetylase Activities in Melanin Biosynthesis

  摘要：

  Melanins are a broad class of darkly pigmented macromolecules formed by oxidative polymerization of phenolic monomers. In fungi, melanins are known virulence factors that contribute to pathogenicity. Their biosynthesis generally involves polymerization of 1,8-dihydroxynaphthalene via a 1,3,6,8-tetrahydroxynaphthalene (THN) precursor assembled by multidomain, nonreducing polyketide synthases. Convergent routes to THN have evolved in fungi. Parallel heptaketide and hexaketide pathways exist that utilize conventional C-terminal thioesterase/Claisen cyclase domains and separate side-chain deacylases. Here, in vitro characterization of Pks1 from Colletotrichum lagenarium establishes a true THN synthase with a bifunctional thioesterase (TE) catalyzing both cyclization and deacetylation of an enzyme-bound hexaketide substrate. Chimeric TE domains were generated by swapping lid regions of active sites between classes of melanin TEs to gain insight into this unprecedented catalysis of carbon-carbon bond making and breaking by an alpha/beta-hydrolase fold enzyme.

  DOI：

  10.1016/j.chembiol.2012.10.002

文献信息

• Illuminating the Diversity of Aromatic Polyketide Synthases in<i>Aspergillus nidulans</i>
  作者：Manmeet Ahuja、Yi-Ming Chiang、Shu-Lin Chang、Mike B. Praseuth、Ruth Entwistle、James F. Sanchez、Hsien-Chun Lo、Hsu-Hua Yeh、Berl R. Oakley、Clay C. C. Wang

  DOI：10.1021/ja3016395

  日期：2012.5.16

  (NR-PKS) genes, key genes in NP biosynthetic pathways, and other genes necessary for NR-PKS product formation or release. This has allowed us to determine the products of eight NR-PKSs of Aspergillus nidulans, including seven novel compounds, as well as the NR-PKS genes required for the synthesis of the toxins alternariol (8) and cichorine (19).

  基因组测序表明，真菌能够合成比目前已知的更多的天然产物 (NPs)，但获得适当表达 NPs 的方法还不够充分。我们已经制定了绕过正常监管机制的成功策略。通过有效的基因靶向，我们已经整体替换了非还原性聚酮化合物合酶 (NR-PKS) 基因的启动子、NP 生物合成途径中的关键基因以及 NR-PKS 产物形成或释放所必需的其他基因。这使我们能够确定构巢曲霉的八种 NR-PKS 的产物，包括七种新化合物，以及合成交链孢菌素 (8) 和菊苣碱 (19) 毒素所需的 NR-PKS 基因。
• Characterization of a Fungal Thioesterase Having Claisen Cyclase and Deacetylase Activities in Melanin Biosynthesis
  作者：Anna L. Vagstad、Eric A. Hill、Jason W. Labonte、Craig A. Townsend

  DOI：10.1016/j.chembiol.2012.10.002

  日期：2012.12

  Melanins are a broad class of darkly pigmented macromolecules formed by oxidative polymerization of phenolic monomers. In fungi, melanins are known virulence factors that contribute to pathogenicity. Their biosynthesis generally involves polymerization of 1,8-dihydroxynaphthalene via a 1,3,6,8-tetrahydroxynaphthalene (THN) precursor assembled by multidomain, nonreducing polyketide synthases. Convergent routes to THN have evolved in fungi. Parallel heptaketide and hexaketide pathways exist that utilize conventional C-terminal thioesterase/Claisen cyclase domains and separate side-chain deacylases. Here, in vitro characterization of Pks1 from Colletotrichum lagenarium establishes a true THN synthase with a bifunctional thioesterase (TE) catalyzing both cyclization and deacetylation of an enzyme-bound hexaketide substrate. Chimeric TE domains were generated by swapping lid regions of active sites between classes of melanin TEs to gain insight into this unprecedented catalysis of carbon-carbon bond making and breaking by an alpha/beta-hydrolase fold enzyme.