ArticleNature chemical biology2024
Enriching productive mutational paths accelerates enzyme evolution.
Article in Nature chemical biology, 2024. 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.
- Graph-based representations in modern protein science.The Biochemical journal · 2026Review
- Enhancing Enzyme Activity With Mutation Combinations Guided by Few-Shot Learning and Causal Inference.Angewandte Chemie (International ed. in English) · 2026Article
- Density Functional Theory Charge Delocalization Error Determines Computed Activation Barriers in Enzymatic Kemp Elimination.Chembiochem : a European journal of chemical biology · 2026Article
- Emergence of specific binding and catalysis from a designed generalist binding protein.Nature chemistry · 2026Article
- Experimental evolution to thermal stress indicates climate resilience in a cosmopolitan arthropod.eLife · 2026Article
- Biomass-Derived Diformylxylose as a Renewable Solvent for Biocatalysis Applications.ChemSusChem · 2026Article
- Low-N Protein Activity Optimization with FolDE.ArXiv · 2025Article
- Of Revolutions and Roadblocks: The Emerging Role of Machine Learning in Biocatalysis.ACS central science · 2025Review
- GeoEvoBuilder: A deep learning framework for efficient functional and thermostable protein design.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Machine learning applied to biocatalysis research.Nature communications · 2025Article
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- Article
- Multi-strategy ugt mining, modification and glycosyl donor synthesis facilitate the production of triterpenoid saponins.Frontiers in plant science · 2025Review
- Enriching productive mutational paths accelerates enzyme evolution.Nature chemical biology · 2024Article
- Spiers Memorial Lecture: Engineering biocatalysts.Faraday discussions · 2024Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Darwinian evolution has given rise to all the enzymes that enable life on Earth. Mimicking natural selection, scientists have learned to tailor these biocatalysts through recursive cycles of mutation, selection and amplification, often relying on screening large protein libraries to productively modulate the complex interplay between protein structure, dynamics and function. Here we show that by removing destabilizing mutations at the library design stage and taking advantage of recent advances in gene synthesis, we can accelerate the evolution of a computationally designed enzyme. In only five rounds of evolution, we generated a Kemp eliminase-an enzymatic model system for proton transfer from carbon-that accelerates the proton abstraction step >10
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.