2-(3,4-Dihydroxybenzoyloxy)-4,6-dihydroxybenzoate

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 缩酚酸和缩酚酸环醚类
• 英文名称: 2-(3,4-Dihydroxybenzoyloxy)-4,6-dihydroxybenzoate
• 英文别名: 4-(2-carboxy-3,5-dihydroxyphenoxy)carbonyl-2-hydroxyphenolate
• 化学式: C14H9O8-
• 分子量: 305.22
• InChiKey: GRXIELRCPYIEQI-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  22
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  147
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  氧气 、 Quercetin-7-olate 生成 2-(3,4-Dihydroxybenzoyloxy)-4,6-dihydroxybenzoate 、 一氧化碳
  参考文献：
  名称：

  Anaerobic enzyme⋅substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase

  摘要：

  橡皮素2,3-双加氧酶（2,3QD）是目前已知唯一确定的铜双加氧酶。它仅依赖于单核铜中心，催化黄酮醇的O-杂环裂解，产生更易降解的酚羧酸酯衍生物。在酶促过程中，同时断裂两个C-C键并释放一氧化碳。已经确定了2,3QD与底物卡培芙醇和天然底物槲皮素在1.90和1.75Å分辨率下的x射线结构，均为无氧复合物。黄酮醇通过它们的3OH基团作为单齿配体与铜离子配位。它们占据了靠近金属中心的浅层和总体上疏水的腔。由于最外层的黄酮醇A环与Pro 164之间的范德华接触，活性位点前的一个灵活环部分有序。有趣的是，结合到2,3QD的黄酮醇在C2原子处弯曲，呈金字塔形。这个原子局部sp3杂化程度的增加可能稳定了一个被活化的碳中心自由基，以便进行双氧攻击。Glu 73通过它的Oɛ1原子配位于铜离子。它的Oɛ2原子与黄酮醇O3原子之间的短距离约为2.55Å，表明两个原子之间存在氢键，表明Glu 73可以在黄酮醇脱质子化时作为碱，并保留质子。基于结构的几何考虑表明，将O2结合到黄酮醇C2原子是黄酮醇双氧化的首选路线。

  DOI：

  10.1073/pnas.262506299

文献信息

• <i>Bacillus subtilis</i>YxaG is a novel Fe-containing quercetin 2,3-dioxygenase
  作者：Laura Bowater、Shirley A Fairhurst、Victoria J Just、Stephen Bornemann

  DOI：10.1016/s0014-5793(03)01439-x

  日期：2004.1.16

  The Bacillus subtilis genome contains genes for three hypothetical proteins belonging to the bicupin family, two of which we have previously shown to be Mn(II)‐dependent oxalate decarboxylases. We have now shown that the third, YxaG, exhibits quercetin 2,3‐dioxygenase activity and that it contains Fe ions. This contrasts with the eukaryotic enzyme which contains a Cu ion. YxaG is the first prokaryotic carbon monoxide‐forming enzyme that utilises a flavonol to be characterised and is only the second example of a prokaryotic dioxygenolytic carbon monoxide‐forming enzyme known to contain a cofactor. It is proposed to rename the B. subtilis gene qdoI.
• Structural and Biochemical Analysis Reveal Pirins to Possess Quercetinase Activity
  作者：Melanie Adams、Zongchao Jia

  DOI：10.1074/jbc.m501034200

  日期：2005.8

  Pirin is a recently identified eukaryotic protein implicated in transcriptional activation and apoptosis. Homologues of Pirin are highly conserved in both prokaryotes and eukaryotes, but their function remains poorly understood. We present here the crystal structure of the yhhW gene product, a putative Pirin homologue, from Escherichia coli and confirm its structural similarity to Pirin. The YhhW protein displays a bicupin fold with a single N-terminal metal coordination site. Molecular surface comparisons of YhhW and Pirin with structurally similar proteins suggested quercetin as a potential ligand. We demonstrate that both bacterial and human Pirins have quercetinase activity, which is inhibited by the addition of typical inhibitors of the quercetin 2,3-dioxygenase reaction. We also demonstrate the release of carbon monoxide as a reaction product. This is the first report of enzymatic activity for any member of the Pirin family and may be an important connection to their roles in transcriptional regulation.
• Quercetinase, a dioxygenase containing copper
  作者：T. Oka、F.J. Simpson

  DOI：10.1016/s0006-291x(71)80076-1

  日期：1971.4