ArticleNature chemistry2018
A designer enzyme for hydrazone and oxime formation featuring an unnatural catalytic aniline residue.
Article in Nature chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 174 citations in OpenAlex.
- Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026Article
- Recoding multiple rare codons enables the simultaneous incorporation of up to five distinct noncanonical amino acids.Nature chemistry · 2026Article
- Building Molecules by a Self-Replicator That Catalyzes Acyl Hydrazone Formation.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering LmrR protein for L-proline-based asymmetric aldol biocatalysis.Nature communications · 2026Article
- Design and evolution of artificial enzyme with in-situ biosynthesized non-canonical amino acid.Nature communications · 2025Article
- Activity-Enhancing Mutations in an LmrR-Based Artificial Metalloenzyme Destabilize the Protein Scaffold and Alter its Conformational Plasticity.Chembiochem : a European journal of chemical biology · 2025Article
- A Genetically Encoded Homocysteine Precursor to Probe Protein Active Sites and to Addict Escherichia coli to a Noncanonical Amino Acid Directly Involved in Catalysis.Angewandte Chemie (International ed. in English) · 2025Article
- Modular multi-enzyme cascades enable green and sustainable synthesis of non-canonical amino acids from glycerol.Nature communications · 2025Article
- Photosensitizer Repositioning Affords an Enantiocomplementary Enzyme for [2 + 2]-Cycloadditions.Angewandte Chemie (International ed. in English) · 2025Article
- Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Directed evolution of aminoacyl-tRNA synthetases through in vivo hypermutation.Nature communications · 2025Article
- Artificial Gold Enzymes Using a Genetically Encoded Thiophenol-Based Noble-Metal-Binding Ligand.Angewandte Chemie (International ed. in English) · 2025Article
- Evolutionary Specialization of a Promiscuous Designer Enzyme.ACS catalysis · 2025Article
- Automated Flow Synthesis of Artificial Heme Enzymes for Enantiodivergent Biocatalysis.Journal of the American Chemical Society · 2025Article
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Machine-Learning-Aided Engineering Hemoglobin as Carbene Transferase for Catalyzing Enantioselective Olefin Cyclopropanation.JACS Au · 2024Article
- Boron Designer Enzyme with a Hybrid Catalytic Dyad.ACS catalysis · 2024Article
- Biosynthesis of Halogenated Tryptophans for Protein Engineering Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024Article
- Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis.Chemical reviews · 2024Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Creating designer enzymes with the ability to catalyse abiological transformations is a formidable challenge. Efforts toward this goal typically consider only canonical amino acids in the initial design process. However, incorporating unnatural amino acids that feature uniquely reactive side chains could significantly expand the catalytic repertoire of designer enzymes. To explore the potential of such artificial building blocks for enzyme design, here we selected p-aminophenylalanine as a potentially novel catalytic residue. We demonstrate that the catalytic activity of the aniline side chain for hydrazone and oxime formation reactions is increased by embedding p-aminophenylalanine into the hydrophobic pore of the multidrug transcriptional regulator from Lactococcus lactis. Both the recruitment of reactants by the promiscuous binding pocket and a judiciously placed aniline that functions as a catalytic residue contribute to the success of the identified artificial enzyme. We anticipate that our design strategy will prove rewarding to significantly expand the catalytic repertoire of designer enzymes in the future.
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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.