A Stilbenoid-Specific Prenyltransferase Utilizes Dimethylallyl Pyrophosphate from the Plastidic Terpenoid Pathway1[OPEN]
A Stilbenoid-Specific Prenyltransferase Utilizes Dimethylallyl Pyrophosphate from the Plastidic Terpenoid Pathway1[OPEN]
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DOI：
10.1104/pp.16.00610
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发表时间：
2016-06
期刊：
影响因子：
7.4
通讯作者：
Tianhong Yang;Lingling Fang;A. Rimando;V. Sobolev;K. Mockaitis;F. Medina-Bolivar
中科院分区：
文献类型：
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作者：
Tianhong Yang;Lingling Fang;A. Rimando;V. Sobolev;K. Mockaitis;F. Medina-Bolivar
二苯乙烯异戊烯基转移酶，利用DMAPP从质体萜类途径显示出高底物特异性。异戊烯化的二苯乙烯类化合物在豆科植物中合成，具有植物抗病性和药理活性，对人类健康具有潜在的益处。尽管它们的重要性，这些化合物的生物合成途径仍有待阐明。花生（Arachis hypogaea）毛状根培养物在用诱导子处理后产生多种异戊二烯化芪类化合物。利用质体和胞质类异戊二烯生物合成途径的代谢抑制剂，我们证明了异戊二烯化芪类化合物上的异戊二烯基部分来自质体途径。我们进一步的特点是，据我们所知，第一次，膜结合的芪特异性异戊二烯转移酶活性从微粒体部分花生毛状根。这种微粒体部分衍生的白藜芦醇4-二甲基烯丙基转移酶利用3，3-二甲基烯丙基焦磷酸作为异戊烯基供体并使白藜芦醇异戊烯化以形成花生素-2。它还prenylates赤松素chiricanine A和piceatannol花生素-5，一个异戊二烯化的芪类化合物确定，据我们所知，在这项研究中的第一次。这种异戊烯基转移酶对二苯乙烯类化合物表现出严格的底物特异性，并且不会异戊烯化黄烷酮、黄酮或异黄酮骨架，尽管它与类黄酮特异性异戊烯基转移酶具有几个共同特征。
Stilbene prenyltransferase that utilizes DMAPP from the plastidic terpenoid pathway shows a high substrate specificity. Prenylated stilbenoids synthesized in some legumes exhibit plant pathogen defense properties and pharmacological activities with potential benefits to human health. Despite their importance, the biosynthetic pathways of these compounds remain to be elucidated. Peanut (Arachis hypogaea) hairy root cultures produce a diverse array of prenylated stilbenoids upon treatment with elicitors. Using metabolic inhibitors of the plastidic and cytosolic isoprenoid biosynthetic pathways, we demonstrated that the prenyl moiety on the prenylated stilbenoids derives from a plastidic pathway. We further characterized, to our knowledge for the first time, a membrane-bound stilbenoid-specific prenyltransferase activity from the microsomal fraction of peanut hairy roots. This microsomal fraction-derived resveratrol 4-dimethylallyl transferase utilizes 3,3-dimethylallyl pyrophosphate as a prenyl donor and prenylates resveratrol to form arachidin-2. It also prenylates pinosylvin to chiricanine A and piceatannol to arachidin-5, a prenylated stilbenoid identified, to our knowledge, for the first time in this study. This prenyltransferase exhibits strict substrate specificity for stilbenoids and does not prenylate flavanone, flavone, or isoflavone backbones, even though it shares several common features with flavonoid-specific prenyltransferases.