ArticleActa crystallographica. Section D, Biological crystallography2013
Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 58 citations in OpenAlex.
- Investigating operational stability and causes of cofactor release in fold type I amine transaminase.Protein science : a publication of the Protein Society · 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
- A transaminase-mediated aldol reaction and applications in cascades to styryl pyridines.Catalysis science & technology · 2024Article
- Construction and yield optimization of a cinnamylamine biosynthesis route in Escherichia coli.Biotechnology for biofuels and bioproducts · 2022Article
- Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay.Journal of mathematical biology · 2020Article
- Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.Scientific reports · 2019Article
- Structural basis of substrate recognition by a novel thermostable (S)-enantioselective ω-transaminase from Thermomicrobium roseum.Scientific reports · 2019Article
- Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution.Frontiers in bioengineering and biotechnology · 2019Article
- Thermostable Branched-Chain Amino Acid Transaminases From the ArchaeaFrontiers in bioengineering and biotechnology · 2019Article
- Single point mutations reveal amino acid residues important for Chromobacterium violaceum transaminase activity in the production of unnatural amino acids.Scientific reports · 2018Article
- Characterization of a Putrescine Transaminase FromFrontiers in bioengineering and biotechnology · 2018Article
- A β-Alanine Catabolism Pathway Containing a Highly Promiscuous ω-Transaminase in the 12-Aminododecanate-Degrading Pseudomonas sp. Strain AAC.Applied and environmental microbiology · 2016Article
- A new target region for changing the substrate specificity of amine transaminases.Scientific reports · 2015Article
- The substrate specificity, enantioselectivity and structure of the (R)-selective amine : pyruvate transaminase from Nectria haematococca.The FEBS journal · 2014Article
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4 authors at 1 institution in 1 country.
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Abstract
The crystal structures and inhibitor complexes of two industrially important ω-aminotransferase enzymes from Pseudomonas aeruginosa and Chromobacterium violaceum have been determined in order to understand the differences in their substrate specificity. The two enzymes share 30% sequence identity and use the same amino acceptor, pyruvate; however, the Pseudomonas enzyme shows activity towards the amino donor β-alanine, whilst the Chromobacterium enzyme does not. Both enzymes show activity towards S-α-methylbenzylamine (MBA), with the Chromobacterium enzyme having a broader substrate range. The crystal structure of the P. aeruginosa enzyme has been solved in the holo form and with the inhibitor gabaculine bound. The C. violaceum enzyme has been solved in the apo and holo forms and with gabaculine bound. The structures of the holo forms of both enzymes are quite similar. There is little conformational difference observed between the inhibitor complex and the holoenzyme for the P. aeruginosa aminotransferase. In comparison, the crystal structure of the C. violaceum gabaculine complex shows significant structural rearrangements from the structures of both the apo and holo forms of the enzyme. It appears that the different rigidity of the protein scaffold contributes to the substrate specificity observed for the two ω-aminotransferases.
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