ArticlePloS one2014
Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 86 citations in OpenAlex.
- Transaminases engineering and their cascade systems for natural product synthesis.Applied biochemistry and biotechnology · 2026Review
- Functional and structural insights into a thermostable (S)-selective amine transaminase and its improved substrate scope by protein engineering.Applied microbiology and biotechnology · 2025Article
- Advances in the Molecular Modification of Microbial ω-Transaminases for Asymmetric Synthesis of Bulky Chiral Amines.Microorganisms · 2025Review
- Computer-aided Drug Discovery Approaches in the Identification of Anticancer Drugs from Natural Products: A Review.Current computer-aided drug design · 2025Review
- Evolving ω-amine transaminaseApplied and environmental microbiology · 2024Article
- Prediction of Thermostability of Enzymes Based on the Amino Acid Index (AAindex) Database and Machine Learning.Molecules (Basel, Switzerland) · 2023Article
- A growth selection system for the directed evolution of amine-forming or converting enzymes.Nature communications · 2022Article
- Engineering Novel (Applied and environmental microbiology · 2022Article
- Computer Modeling Explains the Structural Reasons for the Difference in Reactivity of Amine Transaminases Regarding Prochiral Methylketones.International journal of molecular sciences · 2022Article
- Non-Canonical Amino Acid-Based Engineering of (Frontiers in chemistry · 2022Article
- 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
- Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.Chembiochem : a European journal of chemical biology · 2021Article
- Improving the Thermostability and Activity of Transaminase FromFrontiers in chemistry · 2021Article
- Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.PloS one · 2021Article
- Reshaping the substrate binding region of (R)-selective ω-transaminase for asymmetric synthesis of (R)-3-amino-1-butanol.Applied microbiology and biotechnology · 2020Article
- An (Frontiers in bioengineering and biotechnology · 2020Article
- A Single Mutation Increases the Thermostability and Activity ofMolecules (Basel, Switzerland) · 2019Article
- Highly efficient production of chiral amines in batch and continuous flow by immobilized ω-transaminases on controlled porosity glass metal-ion affinity carrier.Journal of biotechnology · 2019Article
- Bioprospecting Reveals Class III ω-Transaminases Converting Bulky Ketones and Environmentally Relevant Polyamines.Applied and environmental microbiology · 2019Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. ω-Transaminases are able to directly synthesize enantiopure chiral amines by catalysing the transfer of an amino group from a primary amino donor to a carbonyl acceptor with pyridoxal 5'-phosphate (PLP) as cofactor. In nature, (S)-selective amine transaminases are more abundant than the (R)-selective enzymes, and therefore more information concerning their structures is available. Here, we present the crystal structure of an (R)-ω-transaminase from Aspergillus terreus determined by X-ray crystallography at a resolution of 1.6 Å. The structure of the protein is a homodimer that displays the typical class IV fold of PLP-dependent aminotransferases. The PLP-cofactor observed in the structure is present in two states (i) covalently bound to the active site lysine (the internal aldimine form) and (ii) as substrate/product adduct (the external aldimine form) and free lysine. Docking studies revealed that (R)-transaminases follow a dual binding mode, in which the large binding pocket can harbour the bulky substituent of the amine or ketone substrate and the α-carboxylate of pyruvate or amino acids, and the small binding pocket accommodates the smaller substituent.
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