Streamlined screening platforms lead to the discovery of pachysiphine synthase from Tabernanthe iboga

© 2024 The Author(s). New Phytologist © 2024 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 244(2024), 4 vom: 16. Okt., Seite 1437-1449
1. Verfasser: Kamileen, Mohamed O (VerfasserIn)
Weitere Verfasser: Nakamura, Yoko, Luck, Katrin, Heinicke, Sarah, Hong, Benke, Colinas, Maite, Lichman, Benjamin R, O'Connor, Sarah E
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Nicotiana benthamiana Tabernanthe iboga alkaloid cytochrome P450 pachysiphine plant biosynthesis plant natural product Cytochrome P-450 Enzyme System 9035-51-2 mehr... Plant Proteins Indole Alkaloids tabersonine 4429-63-4 Quinolines
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100 1 |a Kamileen, Mohamed O  |e verfasserin  |4 aut 
245 1 0 |a Streamlined screening platforms lead to the discovery of pachysiphine synthase from Tabernanthe iboga 
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520 |a Plant-specialized metabolism is largely driven by the oxidative tailoring of key chemical scaffolds catalyzed by cytochrome P450 (CYP450s) enzymes. Monoterpene indole alkaloids (MIAs) tabersonine and pseudo-tabersonine, found in the medicinal plant Tabernanthe iboga (commonly known as iboga), are tailored with oxidations, and the enzymes involved remain unknown. Here, we developed a streamlined screening strategy to test the activity of T. iboga CYP450s in Nicotiana benthamiana. Using multigene constructs encoding the biosynthesis of tabersonine and pseudo-tabersonine scaffolds, we aimed to uncover the CYP450s responsible for oxidative transformations in these scaffolds. Our approach identified two T. iboga cytochrome P450 enzymes: pachysiphine synthase (PS) and 16-hydroxy-tabersonine synthase (T16H). These enzymes catalyze an epoxidation and site-specific hydroxylation of tabersonine to produce pachysiphine and 16-OH-tabersonine, respectively. This work provides new insights into the biosynthetic pathways of MIAs and underscores the utility of N. benthamiana and Catharanthus roseus as platforms for the functional characterization of plant enzymes 
650 4 |a Journal Article 
650 4 |a Nicotiana benthamiana 
650 4 |a Tabernanthe iboga 
650 4 |a alkaloid 
650 4 |a cytochrome P450 
650 4 |a pachysiphine 
650 4 |a plant biosynthesis 
650 4 |a plant natural product 
650 7 |a Cytochrome P-450 Enzyme System  |2 NLM 
650 7 |a 9035-51-2  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Indole Alkaloids  |2 NLM 
650 7 |a tabersonine  |2 NLM 
650 7 |a 4429-63-4  |2 NLM 
650 7 |a Quinolines  |2 NLM 
700 1 |a Nakamura, Yoko  |e verfasserin  |4 aut 
700 1 |a Luck, Katrin  |e verfasserin  |4 aut 
700 1 |a Heinicke, Sarah  |e verfasserin  |4 aut 
700 1 |a Hong, Benke  |e verfasserin  |4 aut 
700 1 |a Colinas, Maite  |e verfasserin  |4 aut 
700 1 |a Lichman, Benjamin R  |e verfasserin  |4 aut 
700 1 |a O'Connor, Sarah E  |e verfasserin  |4 aut 
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773 1 8 |g volume:244  |g year:2024  |g number:4  |g day:16  |g month:10  |g pages:1437-1449 
856 4 0 |u http://dx.doi.org/10.1111/nph.20133  |3 Volltext 
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