ArticleApplied microbiology and biotechnology2019
Characterisation of a solvent-tolerant haloarchaeal (R)-selective transaminase isolated from a Triassic period salt mine.
Article in Applied microbiology and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Characterization and substrate specificity study of the novel (R)-amine transaminase MagAT.Biotechnology letters · 2025Article
- Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase fromACS omega · 2021Article
- Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.Chembiochem : a European journal of chemical biology · 2021Article
- Transaminases for industrial biocatalysis: novel enzyme discovery.Applied microbiology and biotechnology · 2020Review
- Reshaping the substrate binding region of (R)-selective ω-transaminase for asymmetric synthesis of (R)-3-amino-1-butanol.Applied microbiology and biotechnology · 2020Article
- Haloferax volcanii for biotechnology applications: challenges, current state and perspectives.Applied microbiology and biotechnology · 2020Review
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Abstract
Transaminase enzymes (TAms) are becoming increasingly valuable in the chemist's toolbox as a biocatalytic route to chiral amines. Despite high profile successes, the lack of (R)-selective TAms and robustness under harsh industrial conditions continue to prove problematic. Herein, we report the isolation of the first haloarchaeal TAm (BC61-TAm) to be characterised for the purposes of pharmaceutical biocatalysis. BC61-TAm is an (R)-selective enzyme, cloned from an extremely halophilic archaeon, isolated from a Triassic period salt mine. Produced using a Haloferax volcanii-based expression model, the resulting protein displays a classic halophilic activity profile, as well as thermotolerance (optimum 50 °C) and organic solvent tolerance. Molecular modelling predicts the putative active site residues of haloarchaeal TAms, with molecular dynamics simulations providing insights on the basis of BC61-TAm's organic solvent tolerance. These results represent an exciting advance in the study of transaminases from extremophiles, providing a possible scaffold for future discovery of biocatalytic enzymes with robust properties.
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