Arginine—tRNA ligase
In enzymology, an arginine-tRNA ligase is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, L-arginine, and tRNA, whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-arginine:tRNAArg ligase . 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. 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.
