Kamileen, Mohamed O., Nakamura, Yoko, Luck, Katrin et al. (5 more authors) (2024) Streamlined screening platforms lead to the discovery of pachysiphine synthase from Tabernanthe iboga. New Phytologist. pp. 1437-1449. ISSN 1469-8137
Abstract
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2024 The Author(s) |
Keywords: | alkaloid,cytochrome P450,Nicotiana benthamiana,pachysiphine,plant biosynthesis,plant natural product,Tabernanthe iboga |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) The University of York > Faculty of Sciences (York) > Biology (York) > Centre for Novel Agricultural Products (CNAP) (York) |
Depositing User: | Pure (York) |
Date Deposited: | 18 Oct 2024 00:06 |
Last Modified: | 23 Jan 2025 00:36 |
Published Version: | https://doi.org/10.1111/nph.20133 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1111/nph.20133 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:218583 |
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