Covalent attachment of aspartic acid to yeast aspartyl-tRNA synthetase induced by the enzyme.
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.
D000596:Amino Acids / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001226:Aspartate-tRNA Ligase / Q000378:metabolism*; D001224:Aspartic Acid / Q000378:metabolism*; D011232:Chemical Precipitation; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000596:Amino Acids; D001224:Aspartic Acid; D000604:Amino Acyl-tRNA Synthetases; D001226:Aspartate-tRNA Ligase