Arginine—tRNA ligase

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Arginine—tRNA ligase
EC no.
CAS no.37205-35-9
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Arginyl tRNA synthetase N terminal domain
PDB 1bs2 EBI.jpg
yeast arginyl-trna synthetase

In enzymology, an arginine—tRNA ligase (EC is an enzyme that catalyzes the chemical reaction

ATP + L-arginine + tRNAArg 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, 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]

Structural studies[edit]

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1BS2, 1F7U, 1F7V, and 1IQ0.


  1. ^ Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D (September 1998). "L-arginine recognition by yeast arginyl-tRNA synthetase". EMBO J. 17 (18): 5438–48. doi:10.1093/emboj/17.18.5438. PMC 1170869. PMID 9736621.

Further reading[edit]

  • ALLENDE CC, ALLENDE JE (1964). "Purification and Substrate Specificity of Arginyl-Ribonucleic Acid Synthetase from Rat Liver". J. Biol. Chem. 239: 1102–6. PMID 14165914.
  • Mehler AH, Mitra SK (1967). "The activation of arginyl transfer ribonucleic acid synthetase by transfer ribonucleic acid". J. Biol. Chem. 242 (23): 5495–9. PMID 12325365.
  • Mitra SK, Mehler AH (1967). "The arginyl transfer ribonucleic acid synthetase of Escherichia coli". J. Biol. Chem. 242 (23): 5491–5494. PMID 12325364.
This article incorporates text from the public domain Pfam and InterPro: IPR005148