3-(All-trans-octaprenyl)benzene-1,2-diol

• 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: 3-(All-trans-octaprenyl)benzene-1,2-diol
• 英文别名: 3-[(2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaenyl]benzene-1,2-diol
• 化学式: C₄₆H₇₀O₂
• 分子量: 655.0
• InChiKey: YNPGYMZVNLIZLD-BQFKTQOQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  16.1
• 重原子数：
  48
• 可旋转键数：
  23
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  40.5
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  3-(All-trans-octaprenyl)benzene-1,2-diol 、 S-腺苷蛋氨酸 生成 2-Octaprenyl-6-methoxyphenol 、 氢(+1)阳离子 、 S-(5'-腺苷)-L-高半胱氨酸
  参考文献：
  名称：

  酵母和大鼠Coq3和大肠杆菌UbiG多肽催化辅酶Q生物合成中的两个O-甲基转移酶步骤。

  摘要：

  泛醌（辅酶Q或Q）是一种脂质，在真核生物的线粒体内膜和原核生物的质膜的电子传输链中起作用。酿酒酵母的Q缺陷突变体在八个COQ基因（coq1-coq8）之一中存在缺陷，无法在不可发酵的碳源上生长。Q的生物合成涉及两个单独的O-甲基化步骤。在酵母中，第一次O-甲基化利用3，4-二羟基-5-六聚戊二烯基苯甲酸作为底物，并被认为是由Coq3p催化的，Coq3p是一种32.7-kDa的蛋白质，与大肠杆菌O-甲基转移酶UbiG的同源性为40％ 。在这项研究中，已经化学合成了对应于第二个O-甲基化步骤的法呢基化类似物demethyl-Q（3）和Q（3），并用于体外研究酵母线粒体中的Q生物合成。酵母和大鼠Coq3p都将脱甲基Q（3）前体识别为底物。另外，纯化了大肠杆菌UbiGp并发现其催化了两个O-甲基化步骤。此外，使用针对酵母Coq3p的抗体来确定Coq3多肽与酵母线粒体内膜的基质侧外围相关。结果表明，

  DOI：

  10.1074/jbc.274.31.21665
• 作为产物：
  描述：

  2-Octaprenylphenol 、 氢(+1)阳离子 、 NADPH(4-) 、 氧气 生成 3-(All-trans-octaprenyl)benzene-1,2-diol 、 水 、 NADP⁺
  参考文献：
  名称：

  Ubiquinone (coenzyme Q) biosynthesis in Escherichia coli: identification of the ubiF gene

  摘要：

  当氧气或硝酸盐是电子受体时，泛醌（辅酶 Q，缩写为 Q）在大肠杆菌的电子传递过程中发挥着重要作用。Q 的生物合成至少涉及九个反应。负责这些羟化反应的酶编码基因 ubiB、ubiH 和 ubiF 分别位于大肠杆菌连接图的 87、66 和 15 分钟处。ubiF 编码的加氧酶在 2-辛烯醇-3-甲基-6-甲氧基-1,4-苯醌醇的碳 5 上引入羟基，形成 2-辛烯醇-3-甲基-5-羟基-6-甲氧基-1,4-苯醌醇。一个 ubiF 突变体不能进行这种转化。根据与 UbiH 的同源性，在染色体的 15 分钟区域确定了一个开放阅读框（orf391），用 PCR 扩增并克隆到 pUC18 质粒中。ubiF突变体与该质粒互补后，恢复了在琥珀酸上生长和合成Q的能力。

  DOI：

  10.1111/j.1574-6968.2000.tb09097.x

文献信息

• ubiI, a New Gene in Escherichia coli Coenzyme Q Biosynthesis, Is Involved in Aerobic C5-hydroxylation
  作者：Mahmoud Hajj Chehade、Laurent Loiseau、Murielle Lombard、Ludovic Pecqueur、Alexandre Ismail、Myriam Smadja、Béatrice Golinelli-Pimpaneau、Caroline Mellot-Draznieks、Olivier Hamelin、Laurent Aussel、Sylvie Kieffer-Jaquinod、Natty Labessan、Frédéric Barras、Marc Fontecave、Fabien Pierrel

  DOI：10.1074/jbc.m113.480368

  日期：2013.7

  Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic

  辅酶 Q（泛醌或 Q）是一种氧化还原活性脂质，存在于从细菌到哺乳动物的生物体中，它在能量产生过程中起着至关重要的作用。Q 生物合成是一个涉及多种蛋白质的复杂途径。在这项工作中，我们表明未表征的保守 visC 基因参与了大肠杆菌中的 Q 生物合成，我们将其重命名为 ubiI。基于遗传和生化实验，我们确定 UbiI 蛋白在 C5-羟基化反应中起作用。ubiI 缺陷的菌株具有低水平的 Q，并积累了一种源自 Q 生物合成途径的化合物，我们对其进行了纯化和表征。我们还证明 UbiI 仅与有氧 Q 生物合成有关，并且在没有氧气的情况下，另一种酶催化 C5-羟基化反应。我们已经解决了截短形式的 UbiI 的晶体结构。该结构与经典的 FAD 依赖性对羟基苯甲酸羟化酶具有许多特征，代表了参与 Q 生物合成的单加氧酶的第一个结构特征。定点诱变证实 UbiI 黄素结合口袋的残基对活性很重要。通过我们对 UbiI
• Evolution of Ubiquinone Biosynthesis: Multiple Proteobacterial Enzymes with Various Regioselectivities To Catalyze Three Contiguous Aromatic Hydroxylation Reactions
  作者：Ludovic Pelosi、Anne-Lise Ducluzeau、Laurent Loiseau、Frédéric Barras、Dominique Schneider、Ivan Junier、Fabien Pierrel

  DOI：10.1128/msystems.00091-16

  日期：2016.8.30

  humans, appeared in an ancestral proteobacterium more than 2 billion years ago. UQ biosynthesis has been studied only in a few model organisms, and thus, the diversity of UQ biosynthesis pathways is largely unknown. In the work reported here, we conducted a phylogenomic analysis of hydroxylases involved in UQ biosynthesis. Our results support the existence of at least two UQ hydroxylases in the proteobacterial

  普遍存在的ATP合酶使用电化学梯度来合成ATP形式的细胞能量。该电化学梯度的产生依赖于脂溶性质子载体，如泛醌（UQ），其用于真核生物和变形细菌的呼吸链中。UQ的生物合成需要在芳环的连续位置进行三个羟基化反应。在大肠杆菌中，称为UbiF，UbiH和UbiI的三种UQ黄素单加氧酶（FMO）中的每一种都修饰芳香环的单个位置。三种羟基化反应/三种蛋白质的这种模式已被接受为UQ生物学的范例。使用系统发育分析，我们发现UbiF，UbiH和UbiI仅在一小部分变形细菌中被检测到，并且我们发现了两种新型的UQ FMO：UbiM，它分布在变形杆菌的alpha，beta和gamma类成员中，而UbiL则仅限于alpha变形细菌的成员。值得注意的是，在少于三个UQ羟化酶编码基因的基因组中发现了ubiL和ubiM基因。我们使用生化方法证明，在UQ生物合成过程中，来自红红螺旋藻的UbiL和脑膜炎奈瑟氏球菌的UbiM
• Characterization and Genetic Analysis of Mutant Strains of <i>Escherichia coli</i> K-12 Accumulating the Ubiquinone Precursors 2-Octaprenyl-6-Methoxy-1,4-Benzoquinone and 2-Octaprenyl-3-Methyl-6-Methoxy-1,4-Benzoquinone
  作者：I. G. Young、L. M. McCann、P. Stroobant、F. Gibson

  DOI：10.1128/jb.105.3.769-778.1971

  日期：1971.3

  The ubiquinone precursors, 2-octaprenyl-6-methoxy-1,4-benzoquinone and 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone, were isolated from ubiquinone-deficient mutants of Escherichia coli and identified by nuclear magnetic resonance and mass spectrometry. Mutants accumulating 2-octaprenyl-6-methoxy-1,4-benzoquinone and 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone were shown to carry mutations in genes designated ubiE and ubiF , respectively. The ubiE gene was shown to be cotransducible with metE (minute 75) and close to two other genes concerned with ubiquinone biosynthesis. The ubiF gene was located close to minute 16 by cotransduction with the lip, gltA , and entA genes.

  泛醌的前体物2-辛基-6-甲氧基-1,4-苯醌和2-辛基-3-甲基-6-甲氧基-1,4-苯醌，从泛醌缺乏的大肠杆菌突变体中分离出来，并通过核磁共振和质谱鉴定。积累2-辛基-6-甲氧基-1,4-苯醌和2-辛基-3-甲基-6-甲氧基-1,4-苯醌的突变体分别被证明携带了被指定为ubiE和ubiF的基因突变。ubiE基因被证明与metE（分钟75）共传导，并靠近另外两个与泛醌生物合成有关的基因。ubiF基因通过与lip、gltA和entA基因的共传导，被定位在分钟16附近。
• Complementation of <i>coq3</i> Mutant Yeast by Mitochondrial Targeting of the <i>Escherichia coli</i> UbiG Polypeptide:  Evidence That UbiG Catalyzes Both <i>O</i>-Methylation Steps in Ubiquinone Biosynthesis
  作者：Adam Y. Hsu、Wayne W. Poon、Jennifer A. Shepherd、David C. Myles、Catherine F. Clarke

  DOI：10.1021/bi9602932

  日期：1996.1.1

  Ubiquinone functions in the mitochondrial electron transport chain, Recent evidence suggests that the reduced form of ubiquinone (ubiquinol) may also function as a lipid soluble antioxidant. The biosynthesis of ubiquinone requires two O-methylation steps. In eukaryotes, the first O-methylation step is carried out by the Coq3 polypeptide, which catalyzes the transfer of a methyl group from S-adenosylmethionine to 3,4-dihydroxy-5-polyprenylbenzoate. In Escherichia coli, 2-polyprenyl-6-hydroxyphenol is the predicted substrate; however, the corresponding O-methyltransferase has not been identified. The second O-methylation step in E. coli, the conversion of demethylubiquinone to ubiquinone, is carried out by the UbiG methyltransferase, which is 40% identical in amino acid sequence with the yeast Coq3 methyltransferase. On the basis of the chemical similarity of the first and last methyl-acceptor substrates and the high degree of amino acid sequence identity between Coq3p and UbiG, the ability of UbiG to catalyze both O-methylation steps was investigated. The current study shows that the ubiG gene is able to restore respiration in the yeast coq3 mutant, provided ubiG; is modified to contain a mitochondrial leader sequence. The mitochondrial targeting of O-methyltransferase activity is an essential feature of the ability to restore respiration and hence ubiquinone biosynthesis in vivo. In vitro import assays show the mitochondrial leader sequence present on Coq3p functions to direct mitochondrial import of Coq3p in vitro and that processing to the mature form requires a membrane potential. In vitro methyltransferase assays with E. coli cell lysates and synthetically prepared farnesylated-substrate analogs indicate that UbiG methylates both the derivative of the eukaryotic intermediate, 3,4-dihydroxy-5-farnesylbenzoate, as well as that of the E. coli intermediate, 2-farnesyl-6-hydroxyphenol. The data presented indicate that the yeast Coq3 polypeptide is located in the mitochondria and that E. coli UbiG catalyzes both O-methylation steps in E. coli.