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EC Number Posttranslational Modification Commentary Reference
Show all pathways known for 6.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.1acetylation tyrosyl-tRNA synthetase (TyrRS) in Escherichia coli is acetylated at multiple lysine residues. Acetylation at K85, K235, and K238 impairs the enzyme activity, by genetic-code-expansion strategy to site-specifically incorporate Nepsilonacetyl-l-lysine into selected positions of TyrRS for in vitro characterization. Lysine residue K355 is never acetylated. Most acetylated lysine residues in TyrRS are sensitive to the Escherichia coli deacetylase CobB but not YcgC, overview. Mapping of acetylated lysine residues on the crystal structure of TyrRS, PDB ID 1VBM 744707
Show all pathways known for 6.1.1.1Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.1proteolytic modification the C-terminal domain of the enzyme, which has cytokine and angiogenic activity and stimulates immune cells, is isolated by proteolytic cleavage or alternative splicing, the mini enzyme is a stimulator of blood vessel development, the full-length enzyme is inactive 650116
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