![cover image](https://wikiwandv2-19431.kxcdn.com/_next/image?url=https://upload.wikimedia.org/wikipedia/commons/thumb/4/44/PDB_1bs2_EBI.jpg/640px-PDB_1bs2_EBI.jpg&w=640&q=50)
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
AMP + diphosphate + L-arginyl-tRNAArg
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 | ||||||||
|
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]