Aspartate–tRNA ligase
| Aspartate–tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.1.1.12 | ||||||||
| CAS no. | 9027-32-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aspartate–tRNA ligase (EC 6.1.1.12) is an enzyme that catalyzes the chemical reaction
- ATP + L-aspartate + tRNAAsp AMP + diphosphate + L-aspartyl-tRNAAsp
The 3 substrates of this enzyme are ATP, L-aspartate, and tRNAAsp, whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNAAsp.
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-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1ASY, PDB: 1ASZ, PDB: 1B8A, PDB: 1C0A, PDB: 1EFW, PDB: 1EOV, PDB: 1EQR, PDB: 1G51, PDB: 1IL2, and PDB: 1L0W.
See also
References
- Gangloff J, Dirheimer G (1973). "Studies on aspartyl-tRNA synthetase from Baker's yeast. I Purification and properties of the enzyme". Biochim. Biophys. Acta. 294 (1): 263–72. doi:10.1016/0005-2787(73)90298-0. PMID 4575961.
- NORTON SJ, RAVEL JM, LEE C, SHIVE W (1963). "Purification and properties of the aspartyl ribonucleic acid synthetase of Lactobacillus arabinosus". J. Biol. Chem. 238: 269–74. doi:10.1016/S0021-9258(19)83990-X. PMID 13939000.