Covalent attachment of aspartic acid to yeast aspartyl‐tRNA synthetase induced by the enzyme

Abstract

Aspartic acid can be covalently linked to yeast aspartyl‐tRNA synthetase and to other proteins, in the absence of tRNA, under conditions where the synthetase activates the amino acid into aspartyl‐adenylate, i.e., in the presence of ATP and MgCl₂. The linkage between aspartic acid and the protein is acid and alkali resistant; thus it is likely a peptide‐like amide bond formed between the activated carboxylate group of aspartic acid and the primary amine function of the side chain of lysine residues.