Streamlined screening platforms lead to the discovery of pachysiphine synthase from Tabernanthe iboga
© 2024 The Author(s). New Phytologist © 2024 New Phytologist Foundation.
| Veröffentlicht in: | The New phytologist. - 1979. - 244(2024), 4 vom: 16. Okt., Seite 1437-1449 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2024
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| 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... |
| Zusammenfassung: | © 2024 The Author(s). New Phytologist © 2024 New Phytologist Foundation. 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 |
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| Beschreibung: | Date Completed 17.10.2024 Date Revised 25.10.2024 published: Print-Electronic RefSeq: AF063850.1, PQ178877, PQ178876 Citation Status MEDLINE |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.20133 |