Convergent Biochemical Pathways for Xanthine Alkaloid Production in Plants Evolved from Ancestral Enzymes with Different Catalytic Properties
| Autor: | Ruiqi Huang, Andrew J. O’Donnell, Todd J. Barkman, Jessica J. Barboline |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
enzyme evolution Biology Caffeine synthase AcademicSubjects/SCI01180 01 natural sciences Substrate Specificity Evolution Molecular 03 medical and health sciences Convergent evolution Gene Duplication Gene duplication Genetics medicine Paullinia convergent evolution Molecular Biology Gene Theobromine Ecology Evolution Behavior and Systematics Discoveries 030304 developmental biology caffeine chemistry.chemical_classification 0303 health sciences Cacao AcademicSubjects/SCI01130 Camellia Methyltransferases Metabolic pathway Enzyme chemistry Evolutionary biology ancestral sequence resurrection Xanthines Mutation Flux (metabolism) 010606 plant biology & botany medicine.drug |
| Zdroj: | Molecular Biology and Evolution |
| ISSN: | 1537-1719 0737-4038 |
| Popis: | Convergent evolution is widespread but the extent to which common ancestral conditions are necessary to facilitate the independent acquisition of similar traits remains unclear. In order to better understand how ancestral biosynthetic catalytic capabilities might lead to convergent evolution of similar modern-day biochemical pathways, we resurrected ancient enzymes of the caffeine synthase (CS) methyltransferases that are responsible for theobromine and caffeine production in flowering plants. Ancestral CS enzymes of Theobroma, Paullinia, and Camellia exhibited similar substrate preferences but these resulted in the formation of different sets of products. From these ancestral enzymes, descendants with similar substrate preference and product formation independently evolved after gene duplication events in Theobroma and Paullinia. Thus, it appears that the convergent modern-day pathways likely originated from ancestral pathways with different inferred flux. Subsequently, the modern-day enzymes originated independently via gene duplication and their convergent catalytic characteristics evolved to partition the multiple ancestral activities by different mutations that occurred in homologous regions of the ancestral proteins. These results show that even when modern-day pathways and recruited genes are similar, the antecedent conditions may be distinctive such that different evolutionary steps are required to generate convergence. |
| Databáze: | OpenAIRE |
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