ArticleNature biotechnology2002
Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently.
Article in Nature biotechnology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
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- Machine Learning-driven Protein Library Design: A Path Toward Smarter Libraries.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Directed evolution of alditol oxidase for the production of optically pure D-glycerate from glycerol in the engineered Escherichia coli.Journal of industrial microbiology & biotechnology · 2021Article
- Orthogonal Bioluminescent Probes from Disubstituted Luciferins.Biochemistry · 2021Article
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- Genetically Engineered Proteins to Improve Biomass Conversion: New Advances and Challenges for Tailoring Biocatalysts.Molecules (Basel, Switzerland) · 2019Review
- Identification of Thermus aquaticus DNA polymerase variants with increased mismatch discrimination and reverse transcriptase activity from a smart enzyme mutant library.Scientific reports · 2019Article
- Desensitizing plant EPSP synthase to glyphosate: Optimized global sequence context accommodates a glycine-to-alanine change in the active site.The Journal of biological chemistry · 2019Article
- Highly active enzymes by automated combinatorial backbone assembly and sequence design.Nature communications · 2018Article
- Statistical Coupling Analysis-Guided Library Design for the Discovery of Mutant Luciferases.Biochemistry · 2018Article
- Creating a more robust 5-hydroxymethylfurfural oxidase by combining computational predictions with a novel effective library design.Biotechnology for biofuels · 2018Article
- Comparison of Five Protein Engineering Strategies for Stabilizing an α/β-Hydrolase.Biochemistry · 2017Article
- Article
- Orthogonal Luciferase-Luciferin Pairs for Bioluminescence Imaging.Journal of the American Chemical Society · 2017Article
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9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
We describe synthetic shuffling, an evolutionary protein engineering technology in which every amino acid from a set of parents is allowed to recombine independently of every other amino acid. With the use of degenerate oligonucleotides, synthetic shuffling provides a direct route from database sequence information to functional libraries. Physical starting genes are unnecessary, and additional design criteria such as optimal codon usage or known beneficial mutations can also be incorporated. We performed synthetic shuffling of 15 subtilisin genes and obtained active and highly chimeric enzymes with desirable combinations of properties that we did not obtain by other directed-evolution methods.
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