ArticleNature communications2022
Metal-responsive regulation of enzyme catalysis using genetically encoded chemical switches.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Mechanistic Insight into Conformational Control of Enzyme Activity by Genetically Encoded Metal-Responsive Switches.Chembiochem : a European journal of chemical biology · 2026Article
- Supramolecularly gated enzymes: On-demand activity switching via host-guest competition for precision tumor therapy.Materials today. Bio · 2026Article
- Chemoenzymatic Cascade Synthesis of Metal-ChelatingChemCatChem · 2025Article
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Accelerated enzyme engineering by machine-learning guided cell-free expression.Nature communications · 2025Article
- Pioneering Role of Nanopore Single-Molecule Sensing in Environmental and Food Surveillance.Biosensors · 2025Review
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- DNA-Regulated Multi-Protein Complement Control.Journal of the American Chemical Society · 2024Article
- Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis.Chemical reviews · 2024Review
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- Dual Noncanonical Amino Acid Incorporation Enabling Chemoselective Protein Modification at Two Distinct Sites in Yeast.Biochemistry · 2023Article
- Strategies for Conditional Regulation of Proteins.JACS Au · 2023Review
- Cell-Free Protein Synthesis of Metalloproteins.Advances in biochemical engineering/biotechnology · 2023Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Dynamic control over protein function is a central challenge in synthetic biology. To address this challenge, we describe the development of an integrated computational and experimental workflow to incorporate a metal-responsive chemical switch into proteins. Pairs of bipyridinylalanine (BpyAla) residues are genetically encoded into two structurally distinct enzymes, a serine protease and firefly luciferase, so that metal coordination biases the conformations of these enzymes, leading to reversible control of activity. Computational analysis and molecular dynamics simulations are used to rationally guide BpyAla placement, significantly reducing experimental workload, and cell-free protein synthesis coupled with high-throughput experimentation enable rapid prototyping of variants. Ultimately, this strategy yields enzymes with a robust 20-fold dynamic range in response to divalent metal salts over 24 on/off switches, demonstrating the potential of this approach. We envision that this strategy of genetically encoding chemical switches into enzymes will complement other protein engineering and synthetic biology efforts, enabling new opportunities for applications where precise regulation of protein function is critical.
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Registered trials
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.