γ-curcumene | 28976-68-3

• 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: γ-curcumene
• 英文别名: gamma-Curcumene；1-methyl-4-[(2R)-6-methylhept-5-en-2-yl]cyclohexa-1,3-diene
• CAS: 28976-68-3
• 化学式: C₁₅H₂₄
• 分子量: 204.356
• InChiKey: NGIVKZGKEPRIGG-CQSZACIVSA-N

物化性质

• 保留指数：
  1474;1472;1480;1482;1470;1474;1474;1473;1474;1473;1463;1472;1474;1472;1470;1461;1481;1460;1480;1474;1473;1473;1470

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  15
• 可旋转键数：
  4
• 环数：
  1.0
• 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

• 作为产物：
  描述：

  farnesyl pyrophosphate 生成 pyrophosphoric acid 、 γ-curcumene
  参考文献：
  名称：

  Conversion of (±/-)-synephrine into p-hydroxyphenylacetaldehyde by Arthrobacter synephrinum. A novel enzymic reaction

  摘要：

  从Arthrobacter synephrinum中部分纯化的酶被发现可以催化(±)-synephrine转化为对羟基苯乙醛和甲基胺。这种酶对synephrine非常特异，并且与单胺氧化酶有明显的区别。

  DOI：

  10.1042/bj1590807

文献信息

• The diverse sesquiterpene profile of patchouli, Pogostemon cablin, is correlated with a limited number of sesquiterpene synthases
  作者：Fabienne Deguerry、Laurence Pastore、Shuiqin Wu、Anthony Clark、Joseph Chappell、Michel Schalk

  DOI：10.1016/j.abb.2006.08.006

  日期：2006.10

  patchouli oil synthase genes. Unexpectedly, only five terpene synthase cDNA genes were isolated. Four of the cDNAs encode for synthases catalyzing the biosynthesis of one major sesquiterpene, including a gamma-curcumene synthase, two germacrene D synthases, and a germacrene A synthase. The fifth cDNA encodes for a patchoulol synthase, which catalyzes the conversion of FPP to patchoulol plus at least

  象狼尾草科中的许多植物一样，Pogostemon cablin（patchouli）会积聚大量的精油。广香油是独特的，因为它由24多种不同的倍半萜组成，而不是由不同的单，倍半萜和二萜化合物混合而成。为了确定这种倍半萜的复杂混合物是否来自相等数量的独特倍半萜烯合酶，我们开发了一种RT-PCR策略来分离和功能表征各个广patch香油合酶基因。出乎意料的是，仅分离出五个萜烯合酶cDNA基因。四个cDNA编码催化一种主要倍半萜生物合成的合成酶，包括γ-姜黄烯合酶，两个two并D合成酶和germ并A合成酶。第五个cDNA编码广patch香酚合酶，催化FPP转化为广patch香酚以及至少13种其他倍半萜烯产品。同样有趣的是，不同的体外反应产物的产量在数量上和质量上都类似于从植物提取的广patch香油中发现的倍半萜的概况，这表明单一的萜烯合酶负责植物中萜烯产物的大量和多样性。
• RNA-seq discovery, functional characterization, and comparison of sesquiterpene synthases from Solanum lycopersicum and Solanum habrochaites trichomes
  作者：Petra M. Bleeker、Eleni A. Spyropoulou、Paul J. Diergaarde、Hanne Volpin、Michiel T. J. De Both、Philipp Zerbe、Joerg Bohlmann、Vasiliki Falara、Yuki Matsuba、Eran Pichersky、Michel A. Haring、Robert C. Schuurink

  DOI：10.1007/s11103-011-9813-x

  日期：2011.11

  Solanum lycopersicum and Solanum habrochaites (f. typicum) accession PI127826 emit a variety of sesquiterpenes. To identify terpene synthases involved in the production of these volatile sesquiterpenes, we used massive parallel pyrosequencing (RNA-seq) to obtain the transcriptome of the stem trichomes from these plants. This approach resulted initially in the discovery of six sesquiterpene synthase cDNAs from S. lycopersicum and five from S. habrochaites. Searches of other databases and the S. lycopersicum genome resulted in the discovery of two additional sesquiterpene synthases expressed in trichomes. The sesquiterpene synthases from S. lycopersicum and S. habrochaites have high levels of protein identity. Several of them appeared to encode for non-functional proteins. Functional recombinant proteins produced germacrenes, β-caryophyllene/α-humulene, viridiflorene and valencene from (E,E)-farnesyl diphosphate. However, the activities of these enzymes do not completely explain the differences in sesquiterpene production between the two tomato plants. RT-qPCR confirmed high levels of expression of most of the S. lycopersicum sesquiterpene synthases in stem trichomes. In addition, one sesquiterpene synthase was induced by jasmonic acid, while another appeared to be slightly repressed by the treatment. Our data provide a foundation to study the evolution of terpene synthases in cultivated and wild tomato.

  番茄（Solanum lycopersicum）和哈勃罗切特番茄（Solanum habrochaites）（f. typicum）的PI127826品系会释放多种倍半萜。为了鉴定参与这些挥发性倍半萜合成的萜合成酶，我们使用大规模平行测序（RNA-seq）获得了这些植物茎毛的转录组。这种方法最初发现了番茄（S. lycopersicum）的6个倍半萜合成酶cDNA和哈勃罗切特番茄（S. habrochaites）的5个倍半萜合成酶cDNA。通过对其他数据库和番茄（S. lycopersicum）基因组的搜索，又发现了2个在茎毛中表达的倍半萜合成酶。番茄（S. lycopersicum）和哈勃罗切特番茄（S. habrochaites）的倍半萜合成酶具有高度的蛋白质同源性。其中一些似乎编码无功能的蛋白质。功能性重组蛋白从（E,E）-法呢基二磷酸酯中产生香豆素、β-石竹烯/α-胡莫烯、绿花烯和瓦伦烯。然而，这些酶的活性并不能完全解释两种番茄植物在倍半萜合成方面的差异。RT-qPCR证实了番茄（S. ly
• Conversion of (±/-)-synephrine into <i>p</i>-hydroxyphenylacetaldehyde by <i>Arthrobacter synephrinum</i>. A novel enzymic reaction
  作者：M Veeraswamy、N A Devi、R K Kutty、P V S Rao

  DOI：10.1042/bj1590807

  日期：1976.12.1

  A partically purified enzyme from Arthrobacter synephrinum was found to catalyse the conversion of (±)-synphrine into p-hydroxyphrenylacetaldehyde and methylamine. The enzyme is highly specific for synephrine and is distinctly different from monoamine oxidase.

  从Arthrobacter synephrinum中部分纯化的酶被发现可以催化(±)-synephrine转化为对羟基苯乙醛和甲基胺。这种酶对synephrine非常特异，并且与单胺氧化酶有明显的区别。
• Purification and properties of synephrinase from Arthrobacter synephrinum
  作者：Veeraswamy Manne、Krishnan R. Kutty、Subba Rao V. Pillarisetti

  DOI：10.1016/0003-9861(86)90428-5

  日期：1986.7

  Synephrinase, an enzyme catalyzing the conversion of (-)-synephrine into p-hydroxyphenylacetaldehyde and methylamine, was purified to apparent homogeneity from the cell-free extracts of Arthrobacter synephrinum grown on (+/-)-synephrine as the sole source of carbon and nitrogen. A 40-fold purification was sufficient to produce synephrinase that is apparently homogeneous as judged by native polyacrylamide

  Synephrinase是一种催化（-）-Synephrine转化为对羟基苯乙醛和甲胺的酶，可以从以（+/-）-Synephrine为唯一碳源的无关节杆菌关节杆菌的无细胞提取物中提纯至明显的均一性。氮。通过天然聚丙烯酰胺凝胶电泳判断，40倍的纯化足以产生看起来是均质的，且比活度为1.8摩尔产物/分钟/毫克蛋白质的合成蛋白。因此，该酶是相对丰富的酶，可能占总蛋白的2.5％之多。该酶本质上需要巯基化合物才能发挥其活性。Mg2 +，Ca2 +和Mn2 +等金属离子刺激了酶的活性。金属螯合剂，硫醇试剂，变性剂和金属离子，例如Zn2 +，Hg2 +，Ag1 +，Cu 2+抑制联蛋白酶活性。除了（-）-丝氨酸，该酶还作用于（+/-）-章鱼胺和β-甲氧基丝氨酸。在反应过程中没有利用分子氧。通过Sephadex G-200色谱法测定的酶的分子量约为156,000。该酶由四个相同的亚基组成，分子量为42,000。
• Evident and latent plasticity across the rice diterpene synthase family with potential implications for the evolution of diterpenoid metabolism in the cereals
  作者：Dana Morrone、Matthew L. Hillwig、Matthew E. Mead、Luke Lowry、D. Bruce Fulton、Reuben J. Peters

  DOI：10.1042/bj20101429

  日期：2011.5.1

  The evolution of natural product biosynthetic pathways can be envisioned to occur via a number of mechanisms. In the present study we provide evidence that latent plasticity plays a role in such metabolic evolution. In particular, rice (Oryza sativa) produces both ent- and syn-CPP (copalyl diphosphate), which are substrates for downstream diterpene synthases. In the present paper we report that several members of this enzymatic family exhibit dual reactivity with some pairing of ent-, syn- or normal CPP stereochemistry. Evident plasticity was observed, as a previously reported ent-sandaracopimaradiene synthase also converts syn-CPP into syn-labda-8(17),12E,14-triene, which can be found in planta. Notably, normal CPP is not naturally found in rice. Thus the presence of diterpene synthases that react with this non-native metabolite reveals latent enzymatic/metabolic plasticity, providing biochemical capacity for utilization of such a novel substrate (i.e. normal CPP) which may arise during evolution, the implications of which are discussed.

  天然产物生物合成途径的进化可通过多种机制实现。本研究提供的证据表明，潜在的可塑性在这种代谢进化中发挥了作用。特别是，水稻（Oryza sativa）同时产生ent-和syn-CPP（共聚二磷酸），它们是下游二萜合成酶的底物。在本文中，我们报告了该酶家族中的几个成员表现出了双重反应性，它们在ent-、syn-或正常 CPP 立体化学上有一些配对。我们观察到了明显的可塑性，因为之前报道的一种ent-sandaracopimaradiene合成酶也能将syn-CPP转化为syn-labda-8(17),12E,14-triene，这在植物体内也能发现。值得注意的是，水稻中并不天然存在正常的 CPP。因此，与这种非本地代谢物发生反应的二萜合成酶的存在揭示了潜在的酶/代谢可塑性，为利用这种可能在进化过程中产生的新型底物（即正常 CPP）提供了生化能力，其意义将在本文中讨论。