ArticleChembiochem : a European journal of chemical biology2021
Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Characterization and substrate specificity study of the novel (R)-amine transaminase MagAT.Biotechnology letters · 2025Article
- Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase fromInternational journal of molecular sciences · 2025Article
- From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the BacteriumBiomolecules · 2024Article
- Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase fromInternational journal of molecular sciences · 2023Article
- Synthesis of Enantiopure Sulfoxides by Concurrent Photocatalytic Oxidation and Biocatalytic Reduction.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Non-Canonical Amino Acid-Based Engineering of (Frontiers in chemistry · 2022Article
- Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.Chembiochem : a European journal of chemical biology · 2021Article
- Modeling Alcohol Dehydrogenase Catalysis in Deep Eutectic Solvent/Water Mixtures.Chembiochem : a European journal of chemical biology · 2020Article
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Authors and funding
10 authors at 5 institutions in 5 countries.
Funding
Abstract
Amine transaminases (ATAs) are used to synthesize enantiomerically pure amines, which are building blocks for pharmaceuticals and agrochemicals. R-selective ATAs belong to the fold type IV PLP-dependent enzymes, and different sequence-, structure- and substrate scope-based features have been identified in the past decade. However, our knowledge is still restricted due to the limited number of characterized (R)-ATAs, with additional bias towards fungal origin. We aimed to expand the toolbox of (R)-ATAs and contribute to the understanding of this enzyme subfamily. We identified and characterized four new (R)-ATAs. The ATA from Exophiala sideris contains a motif characteristic for d-ATAs, which was previously believed to be a disqualifying factor for (R)-ATA activity. The crystal structure of the ATA from Shinella is the first from a Gram-negative bacterium. The ATAs from Pseudonocardia acaciae and Tetrasphaera japonica are the first characterized (R)-ATAs with a shortened/missing N-terminal helix. The active-site charges vary significantly between the new and known ATAs, correlating with their diverging substrate scope.
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