Journal
EXTREMOPHILES
Volume 20, Issue 2, Pages 215-225Publisher
SPRINGER JAPAN KK
DOI: 10.1007/s00792-016-0816-z
Keywords
Archaea; Branched-chain amino acid aminotransferase; Selectivity; 3D structure; Thermostability
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Funding
- Russian Science Foundation [14-24-00172]
- ERA-IB project THERMOGENE through the ERA-NET of EU by Russian Foundation
- Russian Science Foundation [14-24-00172] Funding Source: Russian Science Foundation
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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 hightemperature 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 angstrom 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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