Arginine-tRNA ligase

In enzymology, an arginine-tRNA ligase is an enzyme that catalyzes the chemical reaction


 * ATP + L-arginine + tRNAArg $$\rightleftharpoons$$ AMP + diphosphate + L-arginyl-tRNAArg

The 3 substrates of this enzyme are ATP, L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg).

This enzyme belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-arginine:tRNAArg 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.

Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes, , , and.