ArticleExtremophiles : life under extreme conditions2016
First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines.
Article in Extremophiles : life under extreme conditions, 2016. 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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9 citing papers in PubMed, 28 citations in OpenAlex.
- To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme fromMolecules (Basel, Switzerland) · 2023Article
- Key Enzymes Involved in the Synthesis of Hops Phytochemical Compounds: From Structure, Functions to Applications.International journal of molecular sciences · 2021Review
- The Uncommon Active Site of D-Amino Acid Transaminase fromMolecules (Basel, Switzerland) · 2021Article
- Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase fromACS omega · 2021Article
- Effect of Ketosubstrate on the Product Yield in the Transamination Reaction Catalyzed by Transaminase from Thermoproteus uzoniensis.Doklady. Biochemistry and biophysics · 2020Article
- Structural basis of substrate recognition by a novel thermostable (S)-enantioselective ω-transaminase from Thermomicrobium roseum.Scientific reports · 2019Article
- Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.Computational and structural biotechnology journal · 2019Review
- Thermostable Branched-Chain Amino Acid Transaminases From the ArchaeaFrontiers in bioengineering and biotechnology · 2019Article
- Improved l-Leucine Production inMolecules (Basel, Switzerland) · 2018Article
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8 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The gene TUZN1299 from the genome of the hyperthermophilic archaeon Thermoproteus uzoniensis encoding a new 32.8 kDa branched-chain amino acid aminotransferase (BCAT) was expressed in Escherichia coli. The recombinant protein TUZN1299 was purified to homogeneity in the PLP-bound form. TUZN1299 was active towards branched-chain amino acids (L-Val, L-Leu, L-Ile) and showed low but detectable activity toward (R)-alpha-methylbenzylamine. The enzyme exhibits high-temperature optimum, thermal stability, and tolerance to organic solvents. The structure of an archaeal BCAT called TUZN1299 was solved for the first time (at 2.0 Å resolution). TUZN1299 has a typical BCAT type IV fold, and the organization of its active site is similar to that of bacterial BCATs. However, there are some differences in the amino acid composition of the active site.
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