botryococcene | 127483-82-3

• 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: botryococcene
• 英文别名: (6E,10S,11E,13R,16E)-2,6,10,13,17,21-hexamethyl-10-vinyldocosa-2,6,11,16,20-pentaene；(10R,13R)-C30 botryococcene；C30 botryococcene；(6E,10S,11E,13R,16E)-10-ethenyl-2,6,10,13,17,21-hexamethyldocosa-2,6,11,16,20-pentaene
• CAS: 127483-82-3
• 化学式: C₃₀H₅₀
• 分子量: 410.727
• InChiKey: LRCNPQXZCZKGDI-OFGMELEWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  11.7
• 重原子数：
  30
• 可旋转键数：
  15
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  0
• 氢给体数：
  0
• 氢受体数：
  0

反应信息

• 作为反应物：
  描述：

  botryococcene 、 S-腺苷蛋氨酸 生成 3,20-Dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene 、 氢(+1)阳离子 、 S-(5'-腺苷)-L-高半胱氨酸
  参考文献：
  名称：

  Functional Identification of Triterpene Methyltransferases from Botryococcus braunii Race B

  摘要：

  Botryococcus braunii race B is a colony-forming, green algae that accumulates triterpene oils in excess of 30% of its dry weight. The composition of the triterpene oils is dominated by dimethylated to tetramethylated forms of botryococcene and squalene. Although unusual mechanisms for the biosynthesis of botryococcene and squalene were recently described, the enzyme(s) responsible for decorating these triterpene scaffolds with methyl substituents were unknown. A transcriptome of B. braunii was screened computationally assuming that the triterpene methyltransferases (TMTs) might resemble the S-adenosyl methionine-dependent enzymes described for methylating the side chain of sterols. Six sterol methyltransferase-like genes were isolated and functionally characterized. Three of these genes when co-expressed in yeast with complementary squalene synthase or botryococcene synthase expression cassettes resulted in the accumulation of mono-and dimethylated forms of both triterpene scaffolds. Surprisingly, TMT-1 and TMT-2 exhibited preference for squalene as the methyl acceptor substrate, whereas TMT-3 showed a striking preference for botryococcene as its methyl acceptor substrate. These in vivo preferences were confirmed with in vitro assays utilizing microsomal preparations from yeast overexpressing the respective genes, which encode for membrane-associated enzymes. Structural examination of the in vivo yeast generated mono-and dimethylated products by NMR identified terminal carbons, C-3 and C-22/C-20, as the atomic acceptor sites for the methyl additions to squalene and botryococcene, respectively. These sites are identical to those previously reported for the triterpenes extracted from the algae. The availability of closely related triterpene methyltransferases exhibiting distinct substrate selectivity and successive catalytic activities provides important tools for investigating the molecular mechanisms responsible for the specificities exhibited by these unique enzymes.

  DOI：

  10.1074/jbc.m111.316059
• 作为产物：
  描述：

  (E)-6,10-dimethyl-5,9-undecadien-1-yne 在 4-二甲氨基吡啶 、 N-碘代丁二酰亚胺 、 copper(l) iodide 、 dimethylsulfide borane complex 、 二异丁基氢化铝 、 silver nitrate 、 三乙胺 、 环己烯 作用下， 以 四氢呋喃 、 乙醚 、 正己烷 、 二氯甲烷 、 丙酮 、 正戊烷 为溶剂， 反应 44.5h， 生成 botryococcene 、 C30葡萄球菌
  参考文献：
  名称：

  烯基环丙烷的非对映选择性开环全合成C30葡萄球菌和表-葡萄球菌

  摘要：

  三烷基铝化合物执行烯基环丙烷的非对映选择性1,6环断裂。这种新的工具可以制备具有两个非对映立体控制效果的，包含两个遥远立构中心的烃类化合物。受葡萄孢菌素生物合成的启发，该方法成功地应用于该三萜及其差向异构体的非对映和对映选择性制备。

  DOI：

  10.1002/anie.201808709

文献信息

• Synthesis of Enantioenriched Tertiary Boronic Esters from Secondary Allylic Carbamates. Application to the Synthesis of C30 Botryococcene
  作者：Alexander P. Pulis、Varinder K. Aggarwal

  DOI：10.1021/ja303022d

  日期：2012.5.2

  reaction has been explored and found to embrace a broad range of both allylic carbamates and boronic esters. The methodology has been applied to an eight-step, stereoselective synthesis of each of the diastereoisomers of C30 botryococcene.

  对映体富集的仲烯丙基氨基甲酸酯已被 sBuLi 去质子化并与硼酸酯反应。与其他亲电试剂相比，观察到了高α-选择性，并且硼酸盐络合物的形成几乎完全保留了立体化学。硼酸酯复合物经历了立体有择的 1,2-迁移，产生了具有更高 er (>98:2) 的叔烯丙基硼酸酯。该反应的范围已被探索并发现包括广泛的烯丙基氨基甲酸酯和硼酸酯。该方法已应用于 C30 葡萄球菌烯的每种非对映异构体的八步立体选择性合成。
• Identification of unique mechanisms for triterpene biosynthesis in <i>Botryococcus braunii</i>
  作者：Tom D. Niehaus、Shigeru Okada、Timothy P. Devarenne、David S. Watt、Vitaliy Sviripa、Joe Chappell

  DOI：10.1073/pnas.1106222108

  日期：2011.7.26

  Botryococcene biosynthesis is thought to resemble that of squalene, a metabolite essential for sterol metabolism in all eukaryotes. Squalene arises from an initial condensation of two molecules of farnesyl diphosphate (FPP) to form presqualene diphosphate (PSPP), which then undergoes a reductive rearrangement to form squalene. In principle, botryococcene could arise from an alternative rearrangement of the

  葡萄球菌烯的生物合成被认为类似于角鲨烯，角鲨烯是所有真核生物中甾醇代谢必不可少的代谢物。角鲨烯由两个分子的二磷酸法呢酯 (FPP) 初始缩合形成二磷酸前角鲨烯 (PSPP)，然后经过还原重排形成角鲨烯。原则上，葡萄球菌烯可以由前角鲨烯中间体的替代重排产生。由于这些提议的相似性，我们预测葡萄球菌烯合酶将类似于角鲨烯合酶，因此从 Botryococcus braunii B 种中分离出类角鲨烯合酶基因。虽然 B. braunii 确实含有至少一种典型的角鲨烯合酶，但其他三种角鲨烯合酶都没有样 (SSL) 基因直接编码葡萄球菌属的生物合成。SSL-1 催化 PSPP 的生物合成，SSL-2 催化双法呢基醚的生物合成，而 SSL-3 似乎不能直接利用 FPP 作为底物。然而，当合成酶样酶的组合在体内和体外混合在一起时，观察到强大的葡萄球菌烯 (SSL-1+SSL-3) 或角鲨烯生物合成 (SSL1
• Correction to Synthesis of Enantioenriched Tertiary Boronic Esters from Secondary Allylic Carbamates. Application to the Synthesis of C30 Botryococcene
  作者：Alexander P. Pulis、Varinder K. Aggarwal

  DOI：10.1021/ja304872j

  日期：2012.7.11
• Total Synthesis of C30 Botryococcene and <i>epi</i> ‐Botryococcene by a Diastereoselective Ring Opening of Alkenylcyclopropanes
  作者：Morgan Cormier、Aurélien de la Torre、Ilan Marek

  DOI：10.1002/anie.201808709

  日期：2018.10

  Trialkylaluminum compounds perform a diastereoselective 1,6‐ring fragmentation of alkenylcyclopropane. This new tool allows the preparation of hydrocarbon compounds containing two distant stereocenters with a good diastereocontrol. Inspired by the biosynthesis of botryococcene this methodology was applied successfully to the diastereo‐ and enantioselective preparation of this triterpene and its epimer

  三烷基铝化合物执行烯基环丙烷的非对映选择性1,6环断裂。这种新的工具可以制备具有两个非对映立体控制效果的，包含两个遥远立构中心的烃类化合物。受葡萄孢菌素生物合成的启发，该方法成功地应用于该三萜及其差向异构体的非对映和对映选择性制备。
• Functional Identification of Triterpene Methyltransferases from Botryococcus braunii Race B
  作者：Tom D. Niehaus、Scott Kinison、Shigeru Okada、Yun-soo Yeo、Stephen A. Bell、Ping Cui、Timothy P. Devarenne、Joe Chappell

  DOI：10.1074/jbc.m111.316059

  日期：2012.3

  Botryococcus braunii race B is a colony-forming, green algae that accumulates triterpene oils in excess of 30% of its dry weight. The composition of the triterpene oils is dominated by dimethylated to tetramethylated forms of botryococcene and squalene. Although unusual mechanisms for the biosynthesis of botryococcene and squalene were recently described, the enzyme(s) responsible for decorating these triterpene scaffolds with methyl substituents were unknown. A transcriptome of B. braunii was screened computationally assuming that the triterpene methyltransferases (TMTs) might resemble the S-adenosyl methionine-dependent enzymes described for methylating the side chain of sterols. Six sterol methyltransferase-like genes were isolated and functionally characterized. Three of these genes when co-expressed in yeast with complementary squalene synthase or botryococcene synthase expression cassettes resulted in the accumulation of mono-and dimethylated forms of both triterpene scaffolds. Surprisingly, TMT-1 and TMT-2 exhibited preference for squalene as the methyl acceptor substrate, whereas TMT-3 showed a striking preference for botryococcene as its methyl acceptor substrate. These in vivo preferences were confirmed with in vitro assays utilizing microsomal preparations from yeast overexpressing the respective genes, which encode for membrane-associated enzymes. Structural examination of the in vivo yeast generated mono-and dimethylated products by NMR identified terminal carbons, C-3 and C-22/C-20, as the atomic acceptor sites for the methyl additions to squalene and botryococcene, respectively. These sites are identical to those previously reported for the triterpenes extracted from the algae. The availability of closely related triterpene methyltransferases exhibiting distinct substrate selectivity and successive catalytic activities provides important tools for investigating the molecular mechanisms responsible for the specificities exhibited by these unique enzymes.