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Arginyl tRNA synthetase N terminal domain
yeast arginyl-trna synthetase
Identifiers
Symbol	Arg_tRNA_synt_N
Pfam	PF03485
InterPro	IPR005148
SCOP2	1f7u / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, an arginine—tRNA ligase (EC 6.1.1.19) is an enzyme that catalyzes the chemical reaction

ATP + L-arginine + tRNAArg ${\displaystyle \rightleftharpoons }$ 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, 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.

Structural studies

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

References

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

• ALLENDE CC, ALLENDE JE (1964). "Purification and Substrate Specificity of Arginyl-Ribonucleic Acid Synthetase from Rat Liver". J. Biol. Chem. 239 (4): 1102–6. doi:10.1016/S0021-9258(18)91397-9. 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. doi:10.1016/S0021-9258(18)99386-5. PMID 12325365.
• Mitra SK, Mehler AH (1967). "The arginyl transfer ribonucleic acid synthetase of Escherichia coli". J. Biol. Chem. 242 (23): 5491–5494. doi:10.1016/S0021-9258(18)99385-3. PMID 12325364.

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• Protein domains
• EC 6.1.1
• Enzymes of known structure
• Ligase stubs