Lineage-specific patterns in the Moraceae family allow identification of convergent P450 enzymes involved in furanocoumarin biosynthesis

© 2025 The Author(s). New Phytologist © 2025 New Phytologist Foundation.

Détails bibliographiques
Publié dans:The New phytologist. - 1979. - 245(2025), 5 vom: 25. März, Seite 2085-2102
Auteur principal: Bouillé, Alexandre (Auteur)
Autres auteurs: Larbat, Romain, Kumari, Rashmi, Olry, Alexandre, Charles, Clément, Nelson, David R, Thornton, Janet, Villard, Cloé, Hehn, Alain
Format: Article en ligne
Langue:English
Publié: 2025
Accès à la collection:The New phytologist
Sujets:Journal Article Moraceae coumarins cytochrome P450 enzyme functional convergence furanocoumarins specialized metabolism Cytochrome P-450 Enzyme System 9035-51-2 Furocoumarins plus... Plant Proteins Umbelliferones
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245 1 0 |a Lineage-specific patterns in the Moraceae family allow identification of convergent P450 enzymes involved in furanocoumarin biosynthesis 
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520 |a Specialized metabolites are molecules involved in plants' interaction with their environment. Elucidating their biosynthetic pathways is a challenging but rewarding task, leading to societal applications and ecological insights. Furanocoumarins emerged multiple times in Angiosperms, raising the question of how different enzymes evolved into catalyzing identical reactions. To identify enzymes producing lineage-specific metabolites, an evolutionary-based approach was developed and applied to furanocoumarin biosynthesis in Ficus carica (Moraceae). This led to the characterization of CYP71B129-131a, three P450 enzymes whose evolution of the function was investigated using phylogenetics, structural comparisons and site-directed mutagenesis. CYP71B129 and CYP71B130,131a were found to hydroxylate umbelliferone (coumarin) and xanthotoxin (furanocoumarin), respectively. Results suggest that CYP71Bs xanthotoxin hydroxylase activity results from duplications and functional divergence of umbelliferone hydroxylase genes. Structural comparisons highlighted an amino acid affecting CYP71Bs substrate specificity, which may play a key role in allowing xanthotoxin hydroxylation in several P450 subfamilies. CYP71B130-131a characterization validates the proposed enzyme-discovery approach, which can be applied to different pathways and help to avoid the classic bottlenecks of specialized metabolism elucidation. The CYP71Bs also exemplify how furanocoumarin-biosynthetic enzymes can stem from coumarin-biosynthetic ones and provides insights into the molecular mechanisms underlying the multiple emergences of xanthotoxin hydroxylation in distant P450 subfamilies 
650 4 |a Journal Article 
650 4 |a Moraceae 
650 4 |a coumarins 
650 4 |a cytochrome P450 
650 4 |a enzyme functional convergence 
650 4 |a furanocoumarins 
650 4 |a specialized metabolism 
650 7 |a Cytochrome P-450 Enzyme System  |2 NLM 
650 7 |a 9035-51-2  |2 NLM 
650 7 |a Furocoumarins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Umbelliferones  |2 NLM 
700 1 |a Larbat, Romain  |e verfasserin  |4 aut 
700 1 |a Kumari, Rashmi  |e verfasserin  |4 aut 
700 1 |a Olry, Alexandre  |e verfasserin  |4 aut 
700 1 |a Charles, Clément  |e verfasserin  |4 aut 
700 1 |a Nelson, David R  |e verfasserin  |4 aut 
700 1 |a Thornton, Janet  |e verfasserin  |4 aut 
700 1 |a Villard, Cloé  |e verfasserin  |4 aut 
700 1 |a Hehn, Alain  |e verfasserin  |4 aut 
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773 1 8 |g volume:245  |g year:2025  |g number:5  |g day:25  |g month:03  |g pages:2085-2102 
856 4 0 |u http://dx.doi.org/10.1111/nph.20381  |3 Volltext 
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