The peptide bond between E292-A293 of Escherichia coli leucyl-tRNA synthetase is essential for its activity

Research was conducted to examine the cleavage of the purified LeuRS into two peptides of 64 and 33 kDa, the location of cleavage site within the large connecting polypeptide (CP1) and the effect of cleavage on function. Results demonstrate that the cleavage of the E2O2-A293 peptide bond in the CP1 domain of LeuRS does not disturb the structure of its active center for the ATP~PP(sub i) exchange reaction, the cleaved enzyme still catalyzing leucine activation.