Tyrosyl‐tRNA Synthetase of <i>Escherichia coli</i>

Abstract

Using purified Escherichia coli tyrosyl‐tRNA synthetase it was found that the enzyme is a dimer containing apparently identical subunits of molecular weight 47000. The study of the complexes formed between the enzyme and its substrates leads to the conclusion that there are two binding sites for tyrosyladenylate as well as for tRNA Tyr per molecule of enzyme. No binding of tyrosine alone could be observed, but a complex with ATP alone was characterized.