ArticleProceedings of the National Academy of Sciences of the United States of America2009
Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Article
- Context-dependent design of induced-fit enzymes using deep learning generates well-expressed, thermally stable and active enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Retracing the Rapid Evolution of an Herbicide-Degrading Enzyme by Protein Engineering.ACS catalysis · 2023Article
- Loop dynamics and the evolution of enzyme activity.Nature reviews. Chemistry · 2023Review
- Article
- Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.Frontiers in molecular biosciences · 2022Article
- Directed Evolution Methods for Enzyme Engineering.Molecules (Basel, Switzerland) · 2021Review
- Evolution, folding, and design of TIM barrels and related proteins.Current opinion in structural biology · 2021Review
- Identification and Analysis of Natural Building Blocks for Evolution-Guided Fragment-Based Protein Design.Journal of molecular biology · 2020Article
- Highly active enzymes by automated combinatorial backbone assembly and sequence design.Nature communications · 2018Article
- Structural and functional innovations in the real-time evolution of new (βα)Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Why reinvent the wheel? Building new proteins based on ready-made parts.Protein science : a publication of the Protein Society · 2016Review
- De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.Cell · 2016Article
- De novo design of a four-fold symmetric TIM-barrel protein with atomic-level accuracy.Nature chemical biology · 2016Article
- Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation.PLoS genetics · 2016Article
- Two independently folding units of Plasmodium profilin suggest evolution via gene fusion.Cellular and molecular life sciences : CMLS · 2015Article
- Design of symmetric TIM barrel proteins from first principles.BMC biochemistry · 2015Article
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Evolutionary relationship of two ancient protein superfolds.Nature chemical biology · 2014Article
- Highly diverse protein library based on the ubiquitous (β/α)₈ enzyme fold yields well-structured proteins through in vitro folding selection.Chembiochem : a European journal of chemical biology · 2013Article
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4 authors.
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Abstract
The generation of high levels of new catalytic activities on natural and artificial protein scaffolds is a major goal of enzyme engineering. Here, we used random mutagenesis and selection in vivo to establish a sugar isomerisation reaction on both a natural (beta alpha)(8)-barrel enzyme and a catalytically inert chimeric (beta alpha)(8)-barrel scaffold, which was generated by the recombination of 2 (beta alpha)(4)-half barrels. The best evolved variants show turnover numbers and substrate affinities that are similar to those of wild-type enzymes catalyzing the same reaction. The determination of the crystal structure of the most proficient variant allowed us to model the substrate sugar in the novel active site and to elucidate the mechanistic basis of the newly established activity. The results demonstrate that natural and inert artificial protein scaffolds can be converted into highly proficient enzymes in the laboratory, and provide insights into the mechanisms of enzyme evolution.
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