Arginyl-tRNA synthetase (ArgRS)

Arginyl-tRNA synthetase (ArgRS) is an essential cytoplasmic enzyme that catalyzes the attachment of L-arginine to its cognate tRNA^Arg^, a key step in the translation of the genetic code during protein synthesis[5][7][1]. It is a member of the class I aminoacyl-tRNA synthetase family and forms part of the multi-synthetase complex (MSC) in higher eukaryotes, interacting with other synthetases and accessory proteins for coordinated activity and regulation[3]. ArgRS uniquely requires the presence of cognate tRNA for amino acid activation and recognizes specific tRNA structural motifs, facilitating precise aminoacylation[4][1][2]. Mutations in the gene encoding ArgRS (RARS/RARS1) are linked to severe neurodevelopmental disorders such as hypomyelination, highlighting its critical role in nervous system development[5]. Although not a direct therapeutic target for small-molecule drugs, its central function in protein synthesis makes it vital for cell viability and a fundamental component in translational and post-translational regulation. Inhibition or dysfunction typically results in cell growth arrest and death, emphasizing the substantial safety concerns associated with direct targeting of this enzyme[1][7][4].

Other names

RARSRARS1arginyl-tRNA synthetase 1DALRD1HLD9arginyl-tRNA ligase, cytoplasmic

Not applicable for specific drugs; theoretically, inhibitors would block protein synthesis by preventing the charging of tRNA^Arg^ with L-arginine