| Arginine—tRNA ligase | |
| Ec Number: | 6.1.1.19 |
| Cas Number: | 37205-35-9 |
| Go Code: | 0004814 |
| Symbol: | Arg_tRNA_synt_N |
| Arginyl tRNA synthetase N terminal domain | |
| Pfam: | PF03485 |
| Interpro: | IPR005148 |
| Scop: | 1f7u |
In enzymology, an arginine—tRNA ligase is an enzyme that catalyzes the chemical reaction
ATP + L-arginine + tRNAArg
\rightleftharpoons
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, 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 (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.[1]
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes,,, and .