ArticleProtein science : a publication of the Protein Society2022
Design and optimization of enzymatic activity in a de novo β-barrel scaffold.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Article
- Atom-level enzyme active site scaffolding using RFdiffusion2.Nature methods · 2026Article
- Modeling protein-small molecule conformational ensembles with PLACER.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Modeling protein-small molecule conformational ensembles with PLACER.bioRxiv : the preprint server for biology · 2025Article
- Parametrically guided design of beta barrels and transmembrane nanopores using deep learning.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- De Novo Design of Proteins for Autocatalytic Isopeptide Bond Formation.Journal of the American Chemical Society · 2025Article
- A Versatile Protein Scaffold Engineered for the Hierarchical Assembly of Robust and Highly Active Enzymes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Cell-Free Systems to Mimic and Expand Metabolism.ACS synthetic biology · 2025Review
- Parametrically guided design of beta barrels and transmembrane nanopores using deep learning.bioRxiv : the preprint server for biology · 2025Article
- Spiers Memorial Lecture: Engineering biocatalysts.Faraday discussions · 2024Article
- Automated in vivo enzyme engineering accelerates biocatalyst optimization.Nature communications · 2024Review
- Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering.ACS central science · 2024Review
- The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Design and optimization of enzymatic activity in a de novo β-barrel scaffold.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
10 authors.
Funding
Abstract
While native scaffolds offer a large diversity of shapes and topologies for enzyme engineering, their often unpredictable behavior in response to sequence modification makes de novo generated scaffolds an exciting alternative. Here we explore the customization of the backbone and sequence of a de novo designed eight stranded β-barrel protein to create catalysts for a retro-aldolase model reaction. We show that active and specific catalysts can be designed in this fold and use directed evolution to further optimize activity and stereoselectivity. Our results support previous suggestions that different folds have different inherent amenability to evolution and this property could account, in part, for the distribution of natural enzymes among different folds.
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