ArticlePLoS genetics2016
Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation.
Article in PLoS genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Experimental evolution reveals bifunctional genetic solutions to loss of trpF in Salmonella enterica.G3 (Bethesda, Md.) · 2026Article
- Systematic discovery of enzyme promiscuity in Escherichia coli using in vitro metabolomics.Communications biology · 2026Article
- Biofilm Formation and Plastic Degradation in Bacteria from Different Environments: Evidence for Phenotypic Acclimation and Metabolic Exaptation.Microorganisms · 2026Article
- Rescaling of Point Charges as a Way to Improve the Simple-to-Use Electrostatic Embedding Scheme Developed to Explore Enzyme Activity with QM-Oriented Software.Journal of chemical information and modeling · 2025Article
- Loop dynamics and the evolution of enzyme activity.Nature reviews. Chemistry · 2023Review
- Article
- A structural signature motif enlightens the origin and diversification of nuclear receptors.PLoS genetics · 2021Article
- How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation.The FEBS journal · 2020Review
- Mutational Pathways and Trade-Offs Between HisA and TrpF Functions: Implications for Evolution via Gene Duplication and Divergence.Frontiers in microbiology · 2020Article
- Evolutionary design principles in metabolism.Proceedings. Biological sciences · 2019Review
- Genomic Enzymology: Web Tools for Leveraging Protein Family Sequence-Function Space and Genome Context to Discover Novel Functions.Biochemistry · 2017Review
- AGeNNT: annotation of enzyme families by means of refined neighborhood networks.BMC bioinformatics · 2017Article
- Article
- Co-occurrence of analogous enzymes determines evolution of a novel (βα)8-isomerase sub-family after non-conserved mutations in flexible loop.The Biochemical journal · 2016Article
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4 authors.
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Abstract
Modern enzymes are highly optimized biocatalysts that process their substrates with extreme efficiency. Many enzymes catalyze more than one reaction; however, the persistence of such ambiguities, their consequences and evolutionary causes are largely unknown. As a paradigmatic case, we study the history of bi-functionality for a time span of approximately two billion years for the sugar isomerase HisA from histidine biosynthesis. To look back in time, we computationally reconstructed and experimentally characterized three HisA predecessors. We show that these ancient enzymes catalyze not only the HisA reaction but also the isomerization of a similar substrate, which is commonly processed by the isomerase TrpF in tryptophan biosynthesis. Moreover, we found that three modern-day HisA enzymes from Proteobacteria and Thermotogae also possess low TrpF activity. We conclude that this bi-functionality was conserved for at least two billion years, most likely without any evolutionary pressure. Although not actively selected for, this trait can become advantageous in the case of a gene loss. Such exaptation is exemplified by the Actinobacteria that have lost the trpF gene but possess the bi-functional HisA homolog PriA, which adopts the roles of both HisA and TrpF. Our findings demonstrate that bi-functionality can perpetuate in the absence of selection for very long time-spans.
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