ArticleScientific reports2018
Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- To PLP or Not to PLP: Stereodivergent Transaminase-Catalyzed Reactions Directed by Kinetic and Thermodynamic Control.The Journal of organic chemistry · 2025Article
- Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.FEBS letters · 2025Article
- A transaminase-mediated aldol reaction and applications in cascades to styryl pyridines.Catalysis science & technology · 2024Article
- Enzymatic synthesis of benzylisoquinoline alkaloids using a parallel cascade strategy and tyrosinase variants.Nature communications · 2022Article
- Comparative Proteomic Analysis for a Putative Pyridoxal Phosphate-Dependent Aminotransferase Required for Virulence in Acidovorax citrulli.The plant pathology journal · 2021Article
- Structural basis of substrate recognition by a novel thermostable (S)-enantioselective ω-transaminase from Thermomicrobium roseum.Scientific reports · 2019Article
- Crystal structure of the apo form of a β-transaminase from Mesorhizobium sp. strain LUK.Protein science : a publication of the Protein Society · 2019Article
- Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution.Frontiers in bioengineering and biotechnology · 2019Article
- Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.Computational and structural biotechnology journal · 2019Review
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Omega (ω)-transaminase catalyzes the transfer of an amino group from a non-α position amino acid, or an amine compound with no carboxylic group, to an amino acceptor, and has been studied intensively because of its high potential utility in industry and pharmatheutics. The ω-transaminase from Vibrio fluvialis JS17 (Vfat) is an amine:pyruvate transaminase capable of the stereo-selective transamination of arylic chiral amines. This enzyme exhibits extraordinary enantio-selectivity, and has a rapid reaction rate for chiral amine substrates. In this study, we report the crystal structure of the apo form of Vfat. The overall structure of Vfat was typical of other class III aminotransferase exhibiting an N-terminal helical domain, a small domain, and a large domain. Interestingly, the two subunits of apo Vfat in the asymmetric unit had different structures. A comparison of the overall structure to other transaminases, revealed that the structures of the N-terminal helical domain and the large domain can be affected by cofactor occupancy, but the structural rearrangement in these regions can occur independently.
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