Tryptophanyl-tRNA synthetase (TrpRS)

Tryptophanyl-tRNA synthetase (TrpRS) is a class I aminoacyl-tRNA synthetase enzyme responsible for catalyzing the attachment of the amino acid tryptophan to its specific tRNA (tRNA^Trp), a fundamental reaction in protein synthesis[1][3][4][6]. The enzyme achieves this by activating tryptophan with ATP to form a tryptophanyl-AMP intermediate, followed by the transfer of tryptophan to the 3' end of the tRNA molecule, ensuring the accurate decoding of genetic information during translation[1][4]. TrpRS is a validated antimicrobial target because of its crucial role in nearly all organisms and structural distinctions between human and microbial homologs[3][6]. In humans, TrpRS also has noncanonical, angiostatic functions, with possible implications in cancer biology and immune modulation[2][3]. Dysfunction or abnormal expression of TrpRS has been linked to disease states, though routine use as a biomarker awaits further research.

Other names

L-tryptophan-tRNA(Trp) ligase (AMP-forming)Tryptophan-tRNA ligaseTryptophan translaseTryptophanyl ribonucleic synthetaseTryptophanyl-tRNA synthaseTryptophanyl-transfer RNA synthetaseTryptophanyl-transfer ribonucleate synthetaseTryptophanyl-transfer ribonucleic acid synthetaseTryptophanyl-transfer ribonucleic synthetase

Amino acid analogues and inhibitors (competitive or allosteric) block tryptophan or ATP binding, inhibiting aminoacylation of tRNATrp and halting protein synthesis. Small-molecule inhibition of angiostatic activity in the human enzyme.