In enzymology, an arginineâÂÂtRNA ligase () is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, -arginine, and tRNA, whereas its 3 products are AMP, diphosphate, and -arginyl-tRNA.
This enzyme belongs to the family of ligases, to be specific those forming carbonâÂÂoxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is -arginine:tRNA ligase (AMP-forming). Other names in common use include arginyl-tRNA synthetase, arginyl-transfer ribonucleate synthetase, arginyl-transfer RNA synthetase, arginyl transfer ribonucleic acid synthetase, arginine-tRNA synthetase, and arginine translase. This enzyme participates in arginine and proline metabolism and aminoacyl-tRNA biosynthesis.
It contains a conserved domain at the N-terminus called arginyl-tRNA synthetase N-terminal domain or additional domain 1 (Add-1). This domain is about 140 residues long and it has been suggested that it is involved in tRNA recognition.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .