2-acetyl-1,3,6,8-tetrahydroxynaphthalene

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 2-acetyl-1,3,6,8-tetrahydroxynaphthalene
• 英文别名: 2-Acetyl-1,3,6,8-tetrahydroxynaphthalene；1-(1,3,6,8-tetrahydroxynaphthalen-2-yl)ethanone
• 化学式: C₁₂H₁₀O₅
• 分子量: 234.208
• InChiKey: FYPSLERIHMOYRN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  17
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  98
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  methyl 2-(2,4-diacetyl-3,5-bis(benzyloxy)phenyl)acetate 在 lithium hexamethyldisilazane 、 palladium on activated charcoal 、 氢气 、 溶剂黄146 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 生成 2-acetyl-1,3,6,8-tetrahydroxynaphthalene
  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

• Sea Urchin Polyketide Synthase SpPks1 Produces the Naphthalene Precursor to Echinoderm Pigments
  作者：Feng Li、Zhenjian Lin、Joshua P. Torres、Eric A. Hill、Dehai Li、Craig A. Townsend、Eric W. Schmidt

  DOI：10.1021/jacs.2c01416

  日期：2022.6.1

  worms, reinforcing their fundamental importance to echinoderm biology. While the animal microbiome is known to produce aromatic polyketides, this work provides biochemical evidence that animals themselves also harbor ancient, convergent, dedicated pathways to carbocyclic aromatic polyketides. More fundamentally, biochemical analysis of SpPks1 begins to define the vast and unexplored biosynthetic space

  地球上几乎每一种动物物种都在其基因组中编码了一种独特的聚酮化合物合酶 (PKS)，但尚未对动物进化枝 PKS 进行生化表征，甚至这些无处不在的酶的化学产物也仅在少数情况下为人所知。最早被鉴定的动物基因组编码的 PKS 基因是来自海胆的SpPks 1。先前的基因敲除实验表明SpPks 1 参与了海胆色素棘轮色素的合成。在这里，我们表达并纯化SpPks1, 进行生化实验以证明海胆蛋白负责合成 2-acetyl-1,3,6,8-tetrahydroxynaphthalene (ATHN)。由于 ATHN 是棘皮色素的合理前体，该结果定义了无处不在的棘皮动物色素的生物合成途径，并改写了先前的棘皮色素生物合成假设。截断实验表明，与迄今为止表征的其他 I 型迭代 PKS 不同，SpPks1仅使用酮酰基合成酶 (KS)、酰基转移酶和酰基载体蛋白结构域产生萘核心，描绘了一类独特的动物非还原芳香族 PKS (aPKS)。KS
• 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.