Abstract
Phenylalanyl-tRNA synthetase from Escherichia coli does not catalyze the [ 14C]phenylalanyl residue transfer from phenylalanyl-adenylate to adenosine either in the presence or absence of homologous tRNA Phe and tRNA Phe −A. When the reaction mixture contained dithiothreitol, radioactive substance was detected having a mobility on HPLC column close to that of aminoacyladenosine. The amount of this product depended on the concentration of dithiothreitol in the mixture. Phenylalanyl residue was suggested to undergo transfer from aminoacyladenylate to dithiothreitol molecule.
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