Staphylococcus aureus tyrosyl-tRNA synthetase (TyrRS or tyrS)

Staphylococcus aureus tyrosyl-tRNA synthetase is an essential bacterial enzyme responsible for linking L-tyrosine to its corresponding tRNA(Tyr) through an ATP-dependent reaction, forming tyrosyl-AMP and subsequently transferring the amino acid to tRNA. This process is fundamental for ribosomal translation and bacterial protein synthesis. TyrRS belongs to the class I aminoacyl-tRNA synthetases, featuring a Rossmann-fold catalytic domain. It has been structurally characterized in complex with several classes of inhibitors, which provided key insights for the development of novel antibiotics. Selective inhibitors of Staphylococcus aureus TyrRS show potent bacteriostatic effects by halting protein synthesis, positioning the enzyme as a promising target in efforts to combat antibiotic resistance in S. aureus infections.

Other names

Tyrosine--tRNA ligaseTyrRStyrS gene product

Inhibition of tyrosyl-tRNA synthetase blocks aminoacylation of tRNA(Tyr), halting protein synthesis and thus bacterial growth. Most inhibitors are competitive, binding at or near the active site or substrate-binding domain.