ArticleNature chemistry2016
Identification of (S)-selective transaminases for the asymmetric synthesis of bulky chiral amines.
Article in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- A cell-free system for 1,6-hexanediamine synthesis using bulk chemical caprolactam as the feedstock.Synthetic and systems biotechnology · 2026Article
- Functional and structural insights into a thermostable (S)-selective amine transaminase and its improved substrate scope by protein engineering.Applied microbiology and biotechnology · 2025Article
- Stereoselective Biosynthesis of Bichiral Amino Alcohols from Diketone via Difunctionalization.ACS omega · 2025Article
- Phase-Separated Multienzyme Condensates for Efficient Synthesis of Imines from Carboxylic Acids with Enhanced Dual-Cofactor Recycling.International journal of molecular sciences · 2025Article
- Advances in the Molecular Modification of Microbial ω-Transaminases for Asymmetric Synthesis of Bulky Chiral Amines.Microorganisms · 2025Review
- The pedal-like loop of (R)-selective transaminases plays a critical role to the functionality of the enzyme.Biotechnology letters · 2025Article
- Enantio-Complementary Synthesis of 2-Substituted Pyrrolidines and Piperidines via Transaminase-Triggered Cyclizations.JACS Au · 2023Article
- Going Full Circle with Organocatalysis and Biocatalysis: The Latent Potential of Cofactor Mimics in Asymmetric Synthesis.The Journal of organic chemistry · 2023Review
- Enantioselective Single and Dual α-C-H Bond Functionalization of Cyclic Amines via Enzymatic Carbene Transfer.Journal of the American Chemical Society · 2023Article
- Ultrahigh-Throughput Screening of an Artificial Metalloenzyme using Double Emulsions.Angewandte Chemie (International ed. in English) · 2022Article
- Recombinant l-Amino Acid Oxidase with Broad Substrate Spectrum for Co-substrate Recycling in (S)-Selective Transaminase-Catalyzed Kinetic Resolutions.Chembiochem : a European journal of chemical biology · 2022Article
- Stereo-Divergent Enzyme Cascades to Convert Racemic 4-Phenyl-2-Butanol into either (S)- or (R)-Corresponding Chiral Amine.Chembiochem : a European journal of chemical biology · 2022Article
- Computer Modeling Explains the Structural Reasons for the Difference in Reactivity of Amine Transaminases Regarding Prochiral Methylketones.International journal of molecular sciences · 2022Article
- Droplet Microfluidics and Directed Evolution of Enzymes: An Intertwined Journey.Angewandte Chemie (International ed. in English) · 2021Review
- Redesign of (R)-Omega-Transaminase and Its Application for Synthesizing Amino Acids with Bulky Side Chain.Applied biochemistry and biotechnology · 2021Article
- The Unexplored Importance of Fleeting Chiral Intermediates in Enzyme-Catalyzed Reactions.Journal of the American Chemical Society · 2021Article
- Computational Redesign of an ω-Transaminase fromACS catalysis · 2021Article
- Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase fromACS omega · 2021Article
- High Regio- and Stereoselective Multi-enzymatic Synthesis of All Phenylpropanolamine Stereoisomers from β-Methylstyrene.Chembiochem : a European journal of chemical biology · 2021Article
- Biocatalytic access to betazole using a one-pot multienzymatic system in continuous flow.Green chemistry : an international journal and green chemistry resource : GC · 2021Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The use of transaminases to access pharmaceutically relevant chiral amines is an attractive alternative to transition-metal-catalysed asymmetric chemical synthesis. However, one major challenge is their limited substrate scope. Here we report the creation of highly active and stereoselective transaminases starting from fold class I. The transaminases were developed by extensive protein engineering followed by optimization of the identified motif. The resulting enzymes exhibited up to 8,900-fold higher activity than the starting scaffold and are highly stereoselective (up to >99.9% enantiomeric excess) in the asymmetric synthesis of a set of chiral amines bearing bulky substituents. These enzymes should therefore be suitable for use in the synthesis of a wide array of potential intermediates for pharmaceuticals. We also show that the motif can be engineered into other protein scaffolds with sequence identities as low as 70%, and as such should have a broad impact in the field of biocatalytic synthesis and enzyme engineering.
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