ArticleAngewandte Chemie (International ed. in English)2016
A Panel of TrpB Biocatalysts Derived from Tryptophan Synthase through the Transfer of Mutations that Mimic Allosteric Activation.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Sequence-based generative AI design of versatile tryptophan synthases.Nature communications · 2026Article
- Promiscuity Guided Evolution of Decarboxylative Aldolases for Synthesis of Tertiary γ-Hydroxy Amino Acids.Angewandte Chemie (International ed. in English) · 2025Article
- A naturally occurring standalone TrpB enzyme provides insights into allosteric communication within tryptophan synthase.Protein science : a publication of the Protein Society · 2025Article
- Chemoenzymatic Cascade Synthesis of Metal-ChelatingChemCatChem · 2025Article
- Asymmetric Synthesis and Biological Evaluation of Both Enantiomers of 5- and 6-Boronotryptophan as Potential Boron Delivery Agents for Boron Neutron Capture Therapy.ACS medicinal chemistry letters · 2024Article
- Continuous evolution of user-defined genes at 1 million times the genomic mutation rate.Science (New York, N.Y.) · 2024Article
- Harnessing conformational dynamics in enzyme catalysis to achieve nature-like catalytic efficiencies: the shortest path map tool for computational enzyme redesign.Faraday discussions · 2024Article
- Tryptophan production by catalysis of a putative tryptophan synthase protein.Archives of microbiology · 2024Article
- A combinatorially complete epistatic fitness landscape in an enzyme active site.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Engineered Biocatalytic Synthesis of β-N-Substituted-α-Amino Acids.Angewandte Chemie (International ed. in English) · 2023Article
- Multiplexed Assessment of Promiscuous Non-Canonical Amino Acid Synthase Activity in a Pyridoxal Phosphate-Dependent Protein Family.ACS catalysis · 2023Article
- Chemoenzymatic Synthesis of Indole-Containing Acyloin Derivatives.Molecules (Basel, Switzerland) · 2023Article
- Estimating conformational heterogeneity of tryptophan synthase with a template-based Alphafold2 approach.Protein science : a publication of the Protein Society · 2022Article
- Biocatalytic Friedel-Crafts Reactions.ChemCatChem · 2022Review
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- Asymmetric Alkylation of Ketones Catalyzed by Engineered TrpB.Angewandte Chemie (International ed. in English) · 2021Article
- A small-molecule chemical interface for molecular programs.Nucleic acids research · 2021Article
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5 authors.
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Abstract
Naturally occurring enzyme homologues often display highly divergent activity with non-natural substrates. Exploiting this diversity with enzymes engineered for new or altered function, however, is laborious because the engineering must be replicated for each homologue. A small set of mutations of the tryptophan synthase β-subunit (TrpB) from Pyrococcus furiosus, which mimics the activation afforded by binding of the α-subunit, was demonstrated to have a similar activating effect in different TrpB homologues with as little as 57 % sequence identity. Kinetic and spectroscopic analyses indicate that the mutations function through the same mechanism: mimicry of α-subunit binding. From these enzymes, we identified a new TrpB catalyst that displays a remarkably broad activity profile in the synthesis of 5-substituted tryptophans. This demonstrates that allosteric activation can be recapitulated throughout a protein family to explore natural sequence diversity for desirable biocatalytic transformations.
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