Two ubiquitous aldo-keto reductases in the genus Papaver support a patchwork model for morphine pathway evolution.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
29 Oct 2024
29 Oct 2024
Historique:
received:
15
04
2024
accepted:
18
10
2024
medline:
30
10
2024
pubmed:
30
10
2024
entrez:
30
10
2024
Statut:
epublish
Résumé
The evolution of morphinan alkaloid biosynthesis in plants of the genus Papaver includes permutation of several processes including gene duplication, fusion, neofunctionalization, and deletion resulting in the present chemotaxonomy. A critical gene fusion event resulting in the key bifunctional enzyme reticuline epimerase (REPI), which catalyzes the stereochemical inversion of (S)-reticuline, was suggested to precede neofunctionalization of downstream enzymes leading to morphine biosynthesis in opium poppy (Papaver somniferum). The ancestrally related aldo-keto reductases 1,2-dehydroreticuline reductase (DRR), which occurs in some species as a component of REPI, and codeinone reductase (COR) catalyze the second and penultimate steps, respectively, in the pathway converting (S)-reticuline to morphine. Orthologs for each enzyme isolated from the transcriptomes of 12 Papaver species were shown to catalyze their respective reactions in species that capture states of the metabolic pathway prior to key evolutionary events, including the gene fusion event leading to REPI, thus suggesting a patchwork model for pathway evolution. Analysis of the structure and substrate preferences of DRR orthologs in comparison with COR orthologs revealed structure-function relationships underpinning the functional latency of DRR and COR orthologs in the genus Papaver, thus providing insights into the molecular events leading to the evolution of the pathway.
Identifiants
pubmed: 39472466
doi: 10.1038/s42003-024-07100-w
pii: 10.1038/s42003-024-07100-w
doi:
Substances chimiques
Morphine
76I7G6D29C
Aldo-Keto Reductases
EC 1.1.1.-
Plant Proteins
0
reticuline
X35Z551WT4
Benzylisoquinolines
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1410Informations de copyright
© 2024. The Author(s).
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