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Sarpagan bridge enzyme has substrate-controlled cyclization and aromatization modes

Thu-Thuy Dang 1 Jakob Franke 1 Ines Soares Teto Carqueijeiro 2 Chloe Langley 1 Vincent Courdavault 2 Sarah O’connor 1
1 John Innes Centre [Norwich]
2 BBV EA 2106 - Biomolécules et biotechnologies végétales
Abstract : Cyclization reactions that create complex polycyclic scaffolds are hallmarks of alkaloid biosynthetic pathways. We present the discovery of three homologous cytochrome P450s from three monoterpene indole alkaloid-producing plants (Rauwolfia serpentina, Gelsemium sempervirens and Catharanthus roseus) that provide entry into two distinct alkaloid classes, the sarpagans and the β-carbolines. Our results highlight how a common enzymatic mechanism, guided by related but structurally distinct substrates, leads to either cyclization or aromatization.
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https://hal-univ-tours.archives-ouvertes.fr/hal-02527530
Contributor : Sébastien Besseau <>
Submitted on : Wednesday, April 1, 2020 - 11:29:16 AM
Last modification on : Saturday, April 25, 2020 - 2:26:55 PM

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Thu-Thuy Dang, Jakob Franke, Ines Soares Teto Carqueijeiro, Chloe Langley, Vincent Courdavault, et al.. Sarpagan bridge enzyme has substrate-controlled cyclization and aromatization modes. Nature Chemical Biology, Nature Publishing Group, 2018, 14 (8), pp.760-763. ⟨10.1038/s41589-018-0078-4⟩. ⟨hal-02527530⟩

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