ArticleNature chemical biology2018
Computational redesign of enzymes for regio- and enantioselective hydroamination.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 187 citations in OpenAlex.
- Unlocking a Nitrosuccinate Lyase for Decarboxylative Enzymatic Hydronitration.Angewandte Chemie (International ed. in English) · 2026Article
- Immobilization of hydroaminase-expressing recombinant Escherichia coli whole-cell biocatalysts for the production of β-alanine.Biotechnology letters · 2026Article
- Tech-Enhanced Synthesis: Exploring the Synergy between Organic Chemistry and Technology.Journal of the American Chemical Society · 2025Review
- Enhanced Stability ofPolymers · 2025Article
- Bioinformatics and Computationally Supported Redesign of Aspartase for β-Alanine Synthesis by Acrylic Acid Hydroamination.ACS catalysis · 2025Article
- Advances in stress-tolerance elements for microbial cell factories.Synthetic and systems biotechnology · 2024Review
- Machine learning-assisted substrate binding pocket engineering based on structural information.Briefings in bioinformatics · 2024Article
- Tailored Viral-like Particles as Drivers of Medical Breakthroughs.International journal of molecular sciences · 2024Review
- Reshaping Phosphatase Substrate Preference for Controlled Biosynthesis Using a "Design-Build-Test-Learn" Framework.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Advances in succinic acid production: the enhancement of COFrontiers in bioengineering and biotechnology · 2024Review
- Review
- Redesigning methionyl-tRNA synthetase for β-methionine activity with adaptive landscape flattening and experiments.Protein science : a publication of the Protein Society · 2023Article
- De Novo Computational Design of a Lipase with Hydrolysis Activity towards Middle-Chained Fatty Acid Esters.International journal of molecular sciences · 2023Article
- Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations.Biomolecules · 2023Article
- Rational design of enzyme activity and enantioselectivity.Frontiers in bioengineering and biotechnology · 2023Review
- Hijacking Chemical Reactions of P450 Enzymes for Altered Chemical Reactions and Asymmetric Synthesis.International journal of molecular sciences · 2022Review
- Computation-Aided Engineering of Cytochrome P450 for the Production of Pravastatin.ACS catalysis · 2022Article
- Alanine synthesized by alanine dehydrogenase enables ammonium-tolerant nitrogen fixation inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- A growth selection system for the directed evolution of amine-forming or converting enzymes.Nature communications · 2022Article
- New Additions to the Arsenal of Biocatalysts for Noncanonical Amino Acid Synthesis.Current opinion in green and sustainable chemistry · 2022Article
Corrections and comments
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Authors and funding
16 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Introduction of innovative biocatalytic processes offers great promise for applications in green chemistry. However, owing to limited catalytic performance, the enzymes harvested from nature's biodiversity often need to be improved for their desired functions by time-consuming iterative rounds of laboratory evolution. Here we describe the use of structure-based computational enzyme design to convert Bacillus sp. YM55-1 aspartase, an enzyme with a very narrow substrate scope, to a set of complementary hydroamination biocatalysts. The redesigned enzymes catalyze asymmetric addition of ammonia to substituted acrylates, affording enantiopure aliphatic, polar and aromatic β-amino acids that are valuable building blocks for the synthesis of pharmaceuticals and bioactive compounds. Without a requirement for further optimization by laboratory evolution, the redesigned enzymes exhibit substrate tolerance up to a concentration of 300 g/L, conversion up to 99%, β-regioselectivity >99% and product enantiomeric excess >99%. The results highlight the use of computational design to rapidly adapt an enzyme to industrially viable reactions.
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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.