- Characterization of a sesquiterpene cyclase from the glandular trichomes of Leucosceptrum canum for sole production of cedrol in Escherichia coli and Nicotiana benthamiana
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Cedrol is an extremely versatile sesquiterpene alcohol that was approved by the Food and Drug Administration of the United States as a flavoring agent or adjuvant and has been commonly used as a flavoring ingredient in cosmetics, foods and medicine. Furthermore, cedrol possesses a wide range of pharmacological properties including sedative, anti-inflammatory and cytotoxic activities. Commercial production of cedrol relies on fractional distillation of cedar wood oils, followed by recrystallization, and little has been reported about its biosynthesis and aspects of synthetic biology. Here, we report the cloning and functional characterization of a cedrol synthase gene (Lc-CedS) from the transcriptome of the glandular trichomes of a woody Lamiaceae plant Leucosceptrum canum. The recombinant Lc-CedS protein catalyzed the in vitro conversion of farnesyl diphosphate into the single product cedrol, suggesting that Lc-CedS is a high-fidelity terpene synthase. Co-expression of Lc-CedS, a farnesyl diphosphate synthase gene and seven genes of the mevalonate (MVA) pathway responsible for converting acetyl-CoA into farnesyl diphosphate in Escherichia coli afforded 363 μg/L cedrol as the sole product under shaking flask conditions. Transient expression of Lc-CedS in Nicotiana benthamiana also resulted in a single product cedrol with a production level of 3.6 μg/g fresh weight. The sole production of cedrol by introducing of Lc-CedS in engineered E. coli and N. benthamiana suggests now alternative production systems using synthetic biology approaches that would better address sufficient supply of cedrol.
- Luo, Fei,Ling, Yi,Li, De-Sen,Tang, Ting,Liu, Yan-Chun,Liu, Yan,Li, Sheng-Hong
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- Stereoselective quenching of cedryl carbocation in epicedrol biosynthesis
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Epicedrol synthase catalyzes the cyclization of achiral diphosphate substrate, (E,E)-farnesyldiphosphate (FPP) into epicedrol. GC-MS analysis of assay extracts obtained by incubating FPP with epicedrol synthase in 21.6 at % H218O buffer showed the molecular ion of 224 for epicedrol. The labeled oxygen study presented here unambiguously demonstrates that the hydroxyl group of the epicedrol synthase enzymatic product, epicedrol, is derived from a water molecule, not from the phosphate moiety of the FPP.
- Shinde, Sandip S.,Navale, Govinda R.,Said, Madhukar S.,Thulasiram, Hirekodathakallu V.
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supporting information
p. 1161 - 1164
(2016/03/09)
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- Process for the preparation of 8,14-cedranoxide
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Processes for the preparation of 8,14-cedranoxide are disclosed, according to which 8,14-cedrane diol is prepared by reducing 8,14-cedranolide by treatment with the aid of diisobutyl-aluminum hydride followed by acid hydrolysis, or 8,14-cedrane diol is cyclized with dimethyl sulfoxide.
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