Regiospecific hydroxylase and O-methyltransferase for the biosynthesis of anticancer alkaloids in Tabernaemontana elegans (toad tree)

Copyright © 2025 The Authors. Published by Elsevier Masson SAS.. All rights reserved.

Détails bibliographiques
Publié dans:Plant physiology and biochemistry : PPB. - 1991. - 227(2025) vom: 01. Sept., Seite 110161
Auteur principal: Mann, Scott Galeung Alexander (Auteur)
Autres auteurs: Richardson, Matthew Bailey, Young, Rochelle Nicola, Deslongchamps, Ghislain, Qu, Yang
Format: Article en ligne
Langue:English
Publié: 2025
Accès à la collection:Plant physiology and biochemistry : PPB
Sujets:Journal Article Methyltransferases EC 2.1.1.- Mixed Function Oxygenases EC 1.- Alkaloids Plant Proteins Secologanin Tryptamine Alkaloids
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245 1 0 |a Regiospecific hydroxylase and O-methyltransferase for the biosynthesis of anticancer alkaloids in Tabernaemontana elegans (toad tree) 
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520 |a Copyright © 2025 The Authors. Published by Elsevier Masson SAS.. All rights reserved. 
520 |a Monoterpenoid indole alkaloids (MIAs) are a structurally diverse class natural products with significant medicinal properties. Bis-MIAs, such as chemotherapeutic vinblastine and anti-autophagic conodurine, are synthesized through enzymatic coupling of monomeric MIAs, often requiring specific modifications to activate reactive centers. In this study, we report the identification and characterization of a regiospecific enzyme pair, coronaridine 11-hydroxylase (TeC11H) and 11-hydroxycoronaridine O-methyltransferase (TeHCOMT), from Tabernaemontana elegans (toad tree). The C11-methoxylation of coronaridine activates C10 and C12 on the indole for subsequent coupling with a vobasinyl monomer, representing a critical transformation in the biosynthesis of a series of 11-methoxycoronaridine derived bis-iboga-vobasinyl MIAs in T. elegans root with potent anticancer and anti-autophagy activities. Biochemical analysis and homology modeling of TeC11H and TeHCOMT, along with their Tabernanthe iboga (iboga) homologs for coronaridine C10-methoxylation, reveal key residues at their highly similar active sites responsible for distinct regioselectivity, demonstrating how coronaridine is oriented to favour C11 or C10 methoxylation. Our discovery sheds light on the coordinated specification of active sites in metabolically linked enzymes during evolutionary adaptation in different lineages. TeC11H and TeHCOMT represent a valuable tool for metabolic engineering, offering new opportunities to biosynthesize anticancer alkaloids and explore the therapeutic potential of novel bis-MIAs 
650 4 |a Journal Article 
650 7 |a Methyltransferases  |2 NLM 
650 7 |a EC 2.1.1.-  |2 NLM 
650 7 |a Mixed Function Oxygenases  |2 NLM 
650 7 |a EC 1.-  |2 NLM 
650 7 |a Alkaloids  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Secologanin Tryptamine Alkaloids  |2 NLM 
700 1 |a Richardson, Matthew Bailey  |e verfasserin  |4 aut 
700 1 |a Young, Rochelle Nicola  |e verfasserin  |4 aut 
700 1 |a Deslongchamps, Ghislain  |e verfasserin  |4 aut 
700 1 |a Qu, Yang  |e verfasserin  |4 aut 
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773 1 8 |g volume:227  |g year:2025  |g day:01  |g month:09  |g pages:110161 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2025.110161  |3 Volltext 
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