Glutamyl transfer ribonucleic acid synthetase from Escherichia coli has been purified to near homogeneity. The enzyme has a molecular weight of 102,000 and contains two dissimilar subunits. The larger one (molecular weight 56,000) catalyzes the acylation of tRNA g lu with glutamate and also the ATP-PPi exchange reaction. This reaction shows an absolute requirement for tRNA g lu. The smaller subunit (molecular weight 46,000) has no detectable enzymatic activity, but protects the catalytically active subunit against heat inactivation.
No takes yet. Share an insight, caveat, or question.
Dieter Söll (1972) studied this question.
Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context: