First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for l-amino acids and R-amines

@article{Boyko2016FirstSO,
  title={First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for l-amino acids and R-amines},
  author={Konstantin M. Boyko and Tatiana N. Stekhanova and Alena Yu. Nikolaeva and Andrey V Mardanov and Andrey L. Rakitin and Nikolai V. Ravin and Ekaterina Yu. Bezsudnova and Vladimir O. Popov},
  journal={Extremophiles},
  year={2016},
  volume={20},
  pages={215-225}
}
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… CONTINUE READING
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From gene to structure: the protein factory of the NBICS Centre of Kurchatov Institute

  • KM Boyko, AV Lipkin, VO Popov, MV Kovalchuk
  • Crystallogr Rep+ 58:442–449
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