| Aspartate—tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.1.1.12 | ||||||||
| CAS no. | 9027-32-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDBPDBePDBsum | ||||||||
| Gene Ontology | AmiGO /QuickGO | ||||||||
| |||||||||
Inenzymology, anaspartate—tRNA ligase (EC6.1.1.12) is anenzyme thatcatalyzes thechemical reaction
The 3substrates of this enzyme areATP,L-aspartate, andtRNA(Asp), whereas its 3products areAMP,diphosphate, andL-aspartyl-tRNA(Asp).
This enzyme belongs to the family ofligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. Thesystematic name of this enzyme class isL-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use includeaspartyl-tRNA synthetase,aspartyl ribonucleic synthetase,aspartyl-transfer RNA synthetase,aspartic acid translase,aspartyl-transfer ribonucleic acid synthetase, andaspartyl ribonucleate synthetase. This enzyme participates inalanine and aspartate metabolism andaminoacyl-trna biosynthesis.
As of late 2007, 10structures have been solved for this class of enzymes, withPDB accession codes1ASY,1ASZ,1B8A,1C0A,1EFW,1EOV,1EQR,1G51,1IL2, and1L0W.
