ArticleScientific reports2016
Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 52 citations in OpenAlex.
- Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase fromInternational journal of molecular sciences · 2025Article
- Crystal structures of the phosphorylation mimics of human cytosolic branched chain aminotransferase.Archives of biochemistry and biophysics · 2025Article
- The pedal-like loop of (R)-selective transaminases plays a critical role to the functionality of the enzyme.Biotechnology letters · 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
- To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme fromMolecules (Basel, Switzerland) · 2023Article
- The BCAT1 CXXC Motif Provides Protection against ROS in Acute Myeloid Leukaemia Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Non-Canonical Amino Acid-Based Engineering of (Frontiers in chemistry · 2022Article
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- The Uncommon Active Site of D-Amino Acid Transaminase fromMolecules (Basel, Switzerland) · 2021Article
- Metabolic bifunctionality of Rv0812 couples folate and peptidoglycan biosynthesis in Mycobacterium tuberculosis.The Journal of experimental medicine · 2021Article
- Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.Chembiochem : a European journal of chemical biology · 2021Article
- Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.PloS one · 2021Article
- Transaminases for industrial biocatalysis: novel enzyme discovery.Applied microbiology and biotechnology · 2020Review
- Characterisation of a solvent-tolerant haloarchaeal (R)-selective transaminase isolated from a Triassic period salt mine.Applied microbiology and biotechnology · 2019Article
- Amine transaminases in chiral amines synthesis: recent advances and challenges.World journal of microbiology & biotechnology · 2017Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates for a broad range of drugs and fine chemicals. Here, we describe the discovery and characterisation of new transaminases from microorganisms which were enriched in selective media containing (R)-amines as sole nitrogen source. While most of the candidate proteins were clearly assigned to known subgroups of the fold IV family of PLP-dependent enzymes by sequence analysis and characterisation of their substrate specificity, some of them did not fit to any of these groups. The structure of one of these enzymes from Curtobacterium pusillum, which can convert d-amino acids and various (R)-amines with high enantioselectivity, was solved at a resolution of 2.4 Å. It shows significant differences especially in the active site compared to other transaminases of the fold IV family and thus indicates the existence of a new subgroup within this family. Although the discovered transaminases were not able to convert ketones in a reasonable time frame, overall, the enrichment-based approach was successful, as we identified two amine transaminases, which convert (R)-amines with high enantioselectivity, and can be used for a kinetic resolution of 1-phenylethylamine and analogues to obtain the (S)-amines with e.e.s >99%.
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