Thermodynamic Analysis of Tyrosyl-tRNA Synthetases Revealed Bacterial-Selective Tyrosine Derivatives

The non-proteinogenic amino acids m-fluorotyrosine and 2,4-dihydroxyphenylalanine demonstrated a respective 6- and 12-fold greater binding affinity to the purified tyrosyl-tRNA synthetase from Escherichia coli than that from human cytosol. The differential binding was identified by probing the substrate selectivity of the two enzymes with structural analogues of tyrosine using a thermodynamic technique.

Automated summary

Using thermodynamic techniques, it was found that the non-proteinogenic amino acids m-fluorotyrosine and 2,4-dihydroxyphenylalanine exhibited higher binding affinity to the tyrosyl-tRNA synthetase from Escherichia coli than to that from human cytosol.