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Arginine—tRNA ligase

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EC number
  
6.1.1.19

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
37205-35-9

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

Arginine—tRNA ligase httpsuploadwikimediaorgwikipediacommonsthu

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.

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

Arginine—tRNA ligase Wikipedia


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