First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for l-amino acids and R-amines |
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| Authors: | Konstantin M. Boyko Tatiana N. Stekhanova Alena Yu. Nikolaeva Andrey V. Mardanov Andrey L. Rakitin Nikolai V. Ravin Ekaterina Yu. Bezsudnova Vladimir O. Popov |
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| Affiliation: | 1.A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences,Moscow,Russian Federation;2.NBICS Centre, National Research Centre “Kurchatov Institute”,Moscow,Russian Federation;3.Institute of Bioengineering, Research Center of Biotechnology of the Russian Academy of Sciences,Moscow,Russian Federation |
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| 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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