Unique animal prenyltransferase with monoterpene synthase activity
Unique animal prenyltransferase with monoterpene synthase activity
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DOI：
10.1007/s00114-009-0521-1
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发表时间：
2009-06-01
影响因子：
--
通讯作者：
Blomquist, Gary J.
中科院分区：
文献类型：
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作者：
Gilg, Anna B.;Tittiger, Claus;Blomquist, Gary J.
单萜类化合物是一种结构多样的天然化合物，在多种生物的化学生态学中发挥着重要作用。香叶基二磷酸合酶是单萜生物合成的关键酶。GPPS是异戊二烯基二磷酸合酶，其催化二甲基烯丙基二磷酸（C-5）和异戊烯基二磷酸（C-5）之间的单一亲电缩合反应以产生香叶基二磷酸（GDP; C-10）。GDP是所有单萜的普遍前体。随后，单萜脱氢酶负责将GDP转化为各种无环、单环和双环单萜产物。在产生信息素的雄性松小蠹（鞘翅目：小蠹科），非环状单萜月桂烯是生产的主要聚集信息素成分，ipsdienol。在这里，我们报告单萜合酶活性与GPPS的I。皮尼。对重组GPPS进行酶测定以确定单萜合酶活性的存在，并通过气相色谱-质谱联用分析反应产物。功能表达的重组酶产生GDP和月桂烯，使GPPS的I。pini是一种双功能酶。这种独特的昆虫异戊二烯二磷酸合酶具有功能可塑性，这是植物萜烯生物合成酶的特征，有助于目前对类异戊二烯途径的产物特异性的理解。
Monoterpenes are structurally diverse natural compounds that play an essential role in the chemical ecology of a wide array of organisms. A key enzyme in monoterpene biosynthesis is geranyl diphosphate synthase (GPPS). GPPS is an isoprenyl diphosphate synthase that catalyzes a single electrophilic condensation reaction between dimethylallyl diphosphate (C-5) and isopentenyl diphosphate (C-5) to produce geranyl diphosphate (GDP; C-10). GDP is the universal precursor to all monoterpenes. Subsequently, monoterpene synthases are responsible for the transformation of GDP to a variety of acyclic, monocyclic, and bicyclic monoterpene products. In pheromone-producing male Ips pini bark beetles (Coleoptera: Scolytidae), the acyclic monoterpene myrcene is required for the production of the major aggregation pheromone component, ipsdienol. Here, we report monoterpene synthase activity associated with GPPS of I. pini. Enzyme assays were performed on recombinant GPPS to determine the presence of monoterpene synthase activity, and the reaction products were analyzed by coupled gas chromatography-mass spectrometry. The functionally expressed recombinant enzyme produced both GDP and myrcene, making GPPS of I. pini a bifunctional enzyme. This unique insect isoprenyl diphosphate synthase possesses the functional plasticity that is characteristic of terpene biosynthetic enzymes of plants, contributing toward the current understanding of product specificity of the isoprenoid pathway.