4-Amino-3-all-trans-hexaprenylbenzoate

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: 4-Amino-3-all-trans-hexaprenylbenzoate
• 英文别名: 4-amino-3-[(2E,6E,10E,14E,18E)-3,7,11,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaenyl]benzoate
• 化学式: C37H54NO2-
• 分子量: 544.8
• InChiKey: ZBVQLNVIBOLJDL-LAAQXVIISA-M

计算性质

• 辛醇/水分配系数(LogP)：
  12.6
• 重原子数：
  40
• 可旋转键数：
  17
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.49
• 拓扑面积：
  66.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  4-Amino-3-all-trans-hexaprenylbenzoate 、 氢(+1)阳离子 、 氧气 、 [2Fe-2S]¹⁺ 生成 4-Amino-5-hydroxy-3-all-trans-hexaprenylbenzoate 、 水 、 [2Fe-2S]²⁺
  参考文献：
  名称：

  Coenzyme Q Biosynthesis: Coq6 Is Required for the C5-Hydroxylation Reaction and Substrate Analogs Rescue Coq6 Deficiency

  摘要：

  Coenzyme Q (Q), an essential component of eukaryotic cells, is synthesized by several enzymes from the precursor 4-hydroxybenzoic acid. Mutations in six of the Q biosynthesis genes cause diseases that can sometimes be ameliorated by oral Q supplementation. We establish here that Coq6, a predicted flavin-dependent monooxygenase, is involved exclusively in the C5-hydroxylation reaction. In an unusual way, the ferredoxin Yah1 and the ferredoxin reductase Arh1 may be the in vivo source of electrons for Coq6. We also show that hydroxylated analogs of 4-hydroxybenzoic acid, such as vanillic acid or 3,4-dihydroxybenzoic acid, restore Q biosynthesis and respiration in a Saccharomyces cerevisiae coq6 mutant. Our results demonstrate that appropriate analogs of 4-hydroxybenzoic acid can bypass a deficient Q biosynthetic enzyme and might be considered for the treatment of some primary Q deficiencies.

  DOI：

  10.1016/j.chembiol.2011.07.008
• 作为产物：
  描述：

  para-aminobenzoate 、 All-trans-hexaprenyl diphosphate(3-) 生成 4-Amino-3-all-trans-hexaprenylbenzoate 、 pyrophosphoric acid
  参考文献：
  名称：

  线粒体铁氧还蛋白和对氨基苯甲酸参与酵母辅酶Q的生物合成

  摘要：

  酵母泛醌或辅酶Q6（Q6）是一种氧化还原活性脂质，在线粒体电子传输链中起关键作用。至少有9种蛋白质（Coq1p–9p）参与了4-羟基苯甲酸酯（4-HB）的Q6生物合成。现在我们显示，线粒体铁氧还蛋白Yah1p和铁氧还蛋白还原酶Arh1p是Q6生物合成所必需的，可能是该途径的第一个羟基化反应。条件Gal-YAH1和Gal-ARH1突变体会积聚3-六异戊烯基-4-羟基苯酚和3-六异戊烯基-4-氨基苯酚。对氨基苯甲酸（pABA）被证明是3-hexaprenyl-4-aminophenol的前体，并与4-HB竞争Coq2p催化的烯丙基化反应。酵母细胞将U-（13C）-pABA转化为13C环标记的Q6，这一结果将pABA鉴定为Q6的新前体，并暗示在Q6生物合成中还会有NH2-OH转化。

  DOI：

  10.1016/j.chembiol.2010.03.014

文献信息

• Coq6 Is Responsible for the C4-deamination Reaction in Coenzyme Q Biosynthesis in Saccharomyces cerevisiae
  作者：Mohammad Ozeir、Ludovic Pelosi、Alexandre Ismail、Caroline Mellot-Draznieks、Marc Fontecave、Fabien Pierrel

  DOI：10.1074/jbc.m115.675744

  日期：2015.10

  The yeast Saccharomyces cerevisiae is able to use para-aminobenzoic acid (pABA) in addition to 4-hydroxybenzoic acid as a precursor of coenzyme Q, a redox lipid essential to the function of the mitochondrial respiratory chain. The biosynthesis of coenzyme Q from pABA requires a deamination reaction at position C4 of the benzene ring to substitute the amino group with an hydroxyl group. We show here that the FAD-dependent monooxygenase Coq6, which is known to hydroxylate position C5, also deaminates position C4 in a reaction implicating molecular oxygen, as demonstrated with labeling experiments. We identify mutations in Coq6 that abrogate the C4-deamination activity, whereas preserving the C5-hydroxylation activity. Several results support that the deletion of Coq9 impacts Coq6, thus explaining the C4-deamination defect observed in Delta coq9 cells. The vast majority of flavin monooxygenases catalyze hydroxylation reactions on a single position of their substrate. Coq6 is thus a rare example of a flavin monooxygenase that is able to act on two different carbon atoms of its C4-aminated substrate, allowing its deamination and ultimately its conversion into coenzyme Q by the other proteins constituting the coenzyme Q biosynthetic pathway.