Molecular cloning and characterization of a Perilla frutescens cytochrome P450 enzyme that catalyzes the later steps of perillaldehyde biosynthesis
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- 伊藤, 美千穂
- Department of Pharmacognosy, Graduate School of Pharmaceutical Science, Kyoto University・Department of Pharmacognosy, College of Pharmacy, Kinjo Gakuin University
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- Ito, Michiho
- Department of Pharmacognosy, Graduate School of Pharmaceutical Science, Kyoto University
抄録
Perilla produces the cyclohexanoid monoterpene perillaldehyde as a major constituent of an essential oil that is accumulated in its glandular trichomes. Perillaldehyde is a marker compound for quality control of soyo and has biological activities such as antibacterial, sedative, or vasodilatory effects. The predicted perillaldehyde formation involves the cyclization of geranyl diphosphate, hydroxylation, and oxidation, and cytochrome P450 plays a crucial role in perillaldehyde biosynthesis. In this study, a cytochrome P450-type enzyme with perillyl alcohol and perillaldehyde synthase activities was isolated by analyzing an expressed sequence tag library from several oil types of pure lines of perilla. A recombinant protein with a sequence that was highly specific for the type of perillaldehyde was expressed in Saccharomyces cerevisiae and evaluated by an in vitro enzymatic reaction. The recombinant protein catalyzed the hydroxylation and oxidation of limonene to perillyl alcohol and perillaldehyde. Cytochrome P450 limonene-7-hydroxylase cDNA from Perilla frutescens has been previously isolated. The cytochrome P450 isolated in this study shares 37% amino-acid identity with the previously isolated enzyme; however, it may have different characteristics.
収録刊行物
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- Phytochemistry
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Phytochemistry 134 26-37, 2017-02
Elsevier BV
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詳細情報 詳細情報について
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- CRID
- 1050845763718256640
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- NII論文ID
- 120006731148
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- ISSN
- 00319422
- 18733700
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- HANDLE
- 2433/244234
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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