2-Octaprenyl-6-methoxyphenol

• 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: 2-Octaprenyl-6-methoxyphenol
• 英文别名: 2-methoxy-6-[(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]phenol
• 化学式: C₄₇H₇₂O₂
• 分子量: 669.1
• InChiKey: MARGKPIMNMASKJ-CMAXTTDKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  16.5
• 重原子数：
  49
• 可旋转键数：
  24
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  29.5
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  2-Octaprenyl-6-methoxyphenol 、 氢(+1)阳离子 、 NADPH(4-) 、 氧气 生成 6-Methoxy-2-octaprenylhydroquinone 、 水 、 NADP⁺
  参考文献：
  名称：

  摘要：

  DOI：
• 作为产物：
  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

文献信息

• 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.
• Yeast and Rat Coq3 and Escherichia coli UbiG Polypeptides Catalyze Both O-Methyltransferase Steps in Coenzyme Q Biosynthesis
  作者：Wayne W. Poon、Robert J. Barkovich、Adam Y. Hsu、Adam Frankel、Peter T. Lee、Jennifer N. Shepherd、David C. Myles、Catherine F. Clarke

  DOI：10.1074/jbc.274.31.21665

  日期：1999.7

  Ubiquinone (coenzyme Q or Q) is a lipid that functions in the electron transport chain in the inner mitochondrial membrane of eukaryotes and the plasma membrane of prokaryotes. Q-deficient mutants of Saccharomyces cerevisiae harbor defects in one of eight COQ genes (coq1-coq8) and are unable to grow on nonfermentable carbon sources. The biosynthesis of Q involves two separate O-methylation steps. In

  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，