Abstract
Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 was isolated, characterized and crystallized. The enzyme is a tetramer of α 2β 2-type structure, its molecular mass being 264 kDa. Molecular masses of the enzyme subunits are 40 (α) and 92 (β) kDa. The optimal temperature conditions of the tRNA Phe aminoacylation, catalyzed by this enzyme, are close to 80°C. K M values for tRNA Phe from E.coli, for tRNA Phe from T. thermophilus HB8, for phenylalanine and ATP, as well as their temperature dependencies were determined. The enzyme crystals were grown by the hanging drop technique at 4°C in the presence of ammonium sulfate.
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