In enzymology, an arginine—tRNA ligase (EC 6.1.1.19) is an enzyme that catalyzes the chemical reaction
| Arginine—tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.1.1.19 | ||||||||
| CAS no. | 37205-35-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Arginyl tRNA synthetase N terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 yeast arginyl-trna synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | Arg_tRNA_synt_N | ||||||||
| Pfam | PF03485 | ||||||||
| InterPro | IPR005148 | ||||||||
| SCOP2 | 1f7u / SCOPe / SUPFAM | ||||||||
| |||||||||
- 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
editAs of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1BS2, 1F7U, 1F7V, and 1IQ0.
References
edit- ^ 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
edit- 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.
