Biology:Arginine–tRNA ligase
| Arginyl tRNA synthetase N terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 yeast arginyl-trna synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | Arg_tRNA_synt_N | ||||||||
| Pfam | PF03485 | ||||||||
| InterPro | IPR005148 | ||||||||
| SCOP2 | 1f7u / SCOPe / SUPFAM | ||||||||
| |||||||||
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 tRNAArg, whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNAArg.
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
- ↑ "L-arginine recognition by yeast arginyl-tRNA synthetase". EMBO J. 17 (18): 5438–48. September 1998. doi:10.1093/emboj/17.18.5438. PMID 9736621.
Further reading
- "Purification and Substrate Specificity of Arginyl-Ribonucleic Acid Synthetase from Rat Liver". J. Biol. Chem. 239 (4): 1102–6. 1964. doi:10.1016/S0021-9258(18)91397-9. PMID 14165914.
- "The activation of arginyl transfer ribonucleic acid synthetase by transfer ribonucleic acid". J. Biol. Chem. 242 (23): 5495–9. 1967. doi:10.1016/S0021-9258(18)99386-5. PMID 12325365.
- "The arginyl transfer ribonucleic acid synthetase of Escherichia coli". J. Biol. Chem. 242 (23): 5491–5494. 1967. doi:10.1016/S0021-9258(18)99385-3. PMID 12325364.
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