ArticleNature communications2023
Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Reprogramming the Rossmann fold signature motif creates orthogonal redox biocatalysts.Nature communications · 2026Article
- Bridging Algorithms and Biocatalysis: Perspectives on AI-Supported Enzyme Engineering.Molecules (Basel, Switzerland) · 2026Review
- A bacterial symbiont and a plant virus enhance insect fitness by inducing physical defenses against fungal parasites.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Creating highly active fluoroacetate dehalogenases via gate-based synergetic chain design.Nature communications · 2026Article
- Unfreezing structural biology for drug discovery.Nature chemical biology · 2026Review
- Investigating operational stability and causes of cofactor release in fold type I amine transaminase.Protein science : a publication of the Protein Society · 2026Article
- Computational rational design of unspecific peroxygenase for C-H oxidation.Science advances · 2026Article
- Computational design of generalist cyclopropanases with stereodivergent selectivity.Nature communications · 2026Article
- First-Principles Modeling of Nitazoxanide Analogues as Prospective PFOR-Targeted Antibacterials.International journal of molecular sciences · 2025Article
- Directed evolution of a beta-lactamase samples a wide variety of conformational states.Protein science : a publication of the Protein Society · 2025Article
- Spatial Coordination Structure-Driven Enzyme-Like Selectivity in Single-Atom Nanozymes.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Advances in uncovering the mechanisms of macromolecular conformational entropy.Nature chemical biology · 2025Review
- Evolving ω-amine transaminaseApplied and environmental microbiology · 2024Article
- Aspartate aminotransferase ofMicrobiology (Reading, England) · 2024Article
- Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure.Protein science : a publication of the Protein Society · 2024Review
- Article
- Sparks of function by de novo protein design.Nature biotechnology · 2024Review
- Design of efficient artificial enzymes using crystallographically-enhanced conformational sampling.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
9 authors.
Funding
Abstract
Structural plasticity of enzymes dictates their function. Yet, our ability to rationally remodel enzyme conformational landscapes to tailor catalytic properties remains limited. Here, we report a computational procedure for tuning conformational landscapes that is based on multistate design of hinge-mediated domain motions. Using this method, we redesign the conformational landscape of a natural aminotransferase to preferentially stabilize a less populated but reactive conformation and thereby increase catalytic efficiency with a non-native substrate, resulting in altered substrate selectivity. Steady-state kinetics of designed variants reveals activity increases with the non-native substrate of approximately 100-fold and selectivity switches of up to 1900-fold. Structural analyses by room-temperature X-ray crystallography and multitemperature nuclear magnetic resonance spectroscopy confirm that conformational equilibria favor the target conformation. Our computational approach opens the door to targeted alterations of conformational states and equilibria, which should facilitate the design of biocatalysts with customized activity and selectivity.
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