lavandulyl diphosphate | 557786-93-3

• 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: lavandulyl diphosphate
• 英文别名: (R)-lavandulyl diphosphate；[(2R)-5-methyl-2-prop-1-en-2-ylhex-4-enyl] phosphono hydrogen phosphate
• CAS: 557786-93-3
• 化学式: C₁₀H₂₀O₇P₂
• 分子量: 314.212
• InChiKey: LHLLBECTIHFNGQ-JTQLQIEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  19
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  113
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  lavandulyl diphosphate 在 calf intestinal phosphatase 、 水 作用下， 反应 1.0h， 生成 熏衣草醇
  参考文献：
  名称：

  通过定点诱变和形态发生研究三齿蒿法呢基二磷酸合酶和菊基二磷酸合酶的结构-功能

  摘要：

  来自 Artemisia tridentata ssp 的法呢基二磷酸合酶 (FPPase) 和菊基二磷酸合酶 (CPPase) 的氨基酸序列。Spiciformis，减去它们的叶绿体靶向区域，71% 相同，90% 相似。FPPase 通过将异戊烯基二磷酸 (IPP) 与二甲基烯丙基二磷酸 (DMAPP) 偶联，然后再与香叶基二磷酸 (GPP) 偶联，有效且选择性地合成“常规”倍半萜类法呢基二磷酸 (FPP)。相比之下，CPPase 是一种低效的混杂酶，它从两个分子的 DMAPP 中合成“不规则”单萜菊酯二磷酸 (CPP)、薰衣草二磷酸 (LPP) 和微量的马可二磷酸 (MPP)，并将 IPP 与 DMAPP 偶联以形成给 GPP。A. tridentata FPPase 和 CPPase 属于链延长蛋白家族 (PF00348)，萜类合酶超家族 (CL0613) 的一个亚群，其成员具有特征性

  DOI：

  10.1021/jacs.7b07608
• 作为产物：
  描述：

  3-甲基丁-2-烯基膦酰磷酸氢酯 在 1,4-dithio-D,L-threitol 、 recombinant Lavandula x intermedia lavandulyl diphosphate synthase 作用下， 以 aq. buffer 为溶剂， 反应 2.2h， 生成 lavandulyl diphosphate
  参考文献：
  名称：

  The Biosynthetic Origin of Irregular Monoterpenes in Lavandula

  摘要：

  Lavender essential oils are constituted predominantly of regular monoterpenes, for example linalool, 1,8-cineole, and camphor. However, they also contain irregular monoterpenes including lavandulol and lavandulyl acetate. Although the majority of genes responsible for the production of regular monoterpenes in lavenders are now known, enzymes (including lavandulyl diphosphate synthase (LPPS)) catalyzing the biosynthesis of irregular monoterpenes in these plants have not been described. Here, we report the isolation and functional characterization of a novel cis-prenyl diphosphate synthase cDNA, termed Lavandula x intermedia lavandulyl diphosphate synthase (LiLPPS), through a homology-based cloning strategy. The LiLPPS ORF, encoding for a 305-amino acid long protein, was expressed in Escherichia coli, and the recombinant protein was purified by nickel-nitrilotriacetic acid affinity chromatography. The approximately 34.5-kDa bacterially produced protein specifically catalyzed the head-to-middle condensation of two dimethylallyl diphosphate units to LPP in vitro with apparent K-m and k(cat) values of 208 +/- 12 mu M and 0.1 s(-1), respectively. LiLPPS is a homodimeric enzyme with a sigmoidal saturation curve and Hill coefficient of 2.7, suggesting a positive co-operative interaction among its catalytic sites. LiLPPS could be used to modulate the production of lavandulol and its derivatives in plants through metabolic engineering.

  DOI：

  10.1074/jbc.m112.431171

文献信息

• Engineering of a Plant Isoprenyl Diphosphate Synthase for Development of Irregular Coupling Activity
  作者：Iryna Gerasymenko、Yuriy V. Sheludko、Ismael Navarro Fuertes、Volker Schmidts、Lara Steinel、Elisabeth Haumann、Heribert Warzecha

  DOI：10.1002/cbic.202100465

  日期：2022.1.5

  A side activity of a regular isoprenyl diphosphate synthase results in two non-head-to-tail terpene structures. For one of them, a cyclobutane planococcyl diphosphate, this is the first example of an efficient enzymatic synthesis. Rational design of the protein allowed for a considerable increase of the irregular activity. The engineered enzyme can be implicated in the sustainable production of insect

  常规异戊二烯基二磷酸合酶的副活性会产生两个非头尾相连的萜烯结构。对于其中的一种，环丁烷平球藻基二磷酸酯，这是有效酶促合成的第一个例子。蛋白质的合理设计使得不规则活性显着增加。该工程酶可参与昆虫信息素的可持续生产，以实现环境友好型害虫防治。
• Structure–Function Studies of <i>Artemisia tridentata</i> Farnesyl Diphosphate Synthase and Chrysanthemyl Diphosphate Synthase by Site-Directed Mutagenesis and Morphogenesis
  作者：J. Scott Lee、Jian-Jung Pan、Gurusankar Ramamoorthy、C. Dale Poulter

  DOI：10.1021/jacs.7b07608

  日期：2017.10.18

  chain-elongation activity, while similar mutations in the active site of FPPase failed to significantly promote formation of significant amounts of irregular monoterpenes. Our results indicate that CPPase, a promiscuous enzyme, is more plastic toward acquiring new activities, whereas FPPase is more resistant. Mutations of residues outside of the α terpene synthase fold are important for acquisition of FPPase

  来自 Artemisia tridentata ssp 的法呢基二磷酸合酶 (FPPase) 和菊基二磷酸合酶 (CPPase) 的氨基酸序列。Spiciformis，减去它们的叶绿体靶向区域，71% 相同，90% 相似。FPPase 通过将异戊烯基二磷酸 (IPP) 与二甲基烯丙基二磷酸 (DMAPP) 偶联，然后再与香叶基二磷酸 (GPP) 偶联，有效且选择性地合成“常规”倍半萜类法呢基二磷酸 (FPP)。相比之下，CPPase 是一种低效的混杂酶，它从两个分子的 DMAPP 中合成“不规则”单萜菊酯二磷酸 (CPP)、薰衣草二磷酸 (LPP) 和微量的马可二磷酸 (MPP)，并将 IPP 与 DMAPP 偶联以形成给 GPP。A. tridentata FPPase 和 CPPase 属于链延长蛋白家族 (PF00348)，萜类合酶超家族 (CL0613) 的一个亚群，其成员具有特征性
• The Biosynthetic Origin of Irregular Monoterpenes in Lavandula
  作者：Zerihun A. Demissie、LaurenA.E. Erland、Mark R. Rheault、Soheil S. Mahmoud

  DOI：10.1074/jbc.m112.431171

  日期：2013.3

  Lavender essential oils are constituted predominantly of regular monoterpenes, for example linalool, 1,8-cineole, and camphor. However, they also contain irregular monoterpenes including lavandulol and lavandulyl acetate. Although the majority of genes responsible for the production of regular monoterpenes in lavenders are now known, enzymes (including lavandulyl diphosphate synthase (LPPS)) catalyzing the biosynthesis of irregular monoterpenes in these plants have not been described. Here, we report the isolation and functional characterization of a novel cis-prenyl diphosphate synthase cDNA, termed Lavandula x intermedia lavandulyl diphosphate synthase (LiLPPS), through a homology-based cloning strategy. The LiLPPS ORF, encoding for a 305-amino acid long protein, was expressed in Escherichia coli, and the recombinant protein was purified by nickel-nitrilotriacetic acid affinity chromatography. The approximately 34.5-kDa bacterially produced protein specifically catalyzed the head-to-middle condensation of two dimethylallyl diphosphate units to LPP in vitro with apparent K-m and k(cat) values of 208 +/- 12 mu M and 0.1 s(-1), respectively. LiLPPS is a homodimeric enzyme with a sigmoidal saturation curve and Hill coefficient of 2.7, suggesting a positive co-operative interaction among its catalytic sites. LiLPPS could be used to modulate the production of lavandulol and its derivatives in plants through metabolic engineering.