Arginine—tRNA ligase

Arginyl tRNA synthetase N terminal domain
yeast arginyl-trna synthetase
Identifiers
Symbol	Arg_tRNA_synt_N
Pfam	PF03485
InterPro	IPR005148
SCOP	1f7u
SUPERFAMILY	1f7u
Available protein structures: Pfam structures 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 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

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

References

Further reading

• 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 and Mehler AH (1967). "The arginyl transfer ribonucleic acid synthetase of Escherichia coli". J. Biol. Chem. 242: 5491–5494. 

This article incorporates text from the public domain Pfam and InterPro IPR005148