Arginine-tRNA ligase

From Wikipedia, the free encyclopedia

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

ATP + L-arginine + tRNAArg $\rightleftharpoons$ 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, specifically 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 6.1.1.19
BRENDA references for 6.1.1.19 (Recommended.)
PubMed references for 6.1.1.19
PubMed Central references for 6.1.1.19
Google Scholar references for 6.1.1.19
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: 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.