Aspartate—ammonia ligase
| Aspartate—ammonia ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.1 | ||||||||
| CAS no. | 9023-69-2 | ||||||||
| 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—ammonia ligase (EC 6.3.1.1) is an enzyme that catalyzes the chemical reaction
- ATP + L-aspartate + NH3 AMP + diphosphate + L-asparagine
The 3 substrates of this enzyme are ATP, L-aspartate, and NH3, whereas its 3 products are AMP, diphosphate, and L-asparagine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (AMP-forming). Other names in common use include asparagine synthetase, and L-asparagine synthetase. This enzyme participates in 3 metabolic pathways: alanine and aspartate metabolism, cyanoamino acid metabolism, and nitrogen metabolism.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes PDB: 11AS and PDB: 12AS.
References
[edit]- RAVEL JM, NORTON SJ, HUMPHREYS JS, SHIVE W (1962). "Asparagine biosynthesis in Lactobacillus arabinosus and its control by asparagine through enzyme inhibition and repression". J. Biol. Chem. 237 (9): 2845–9. doi:10.1016/S0021-9258(18)60238-8. PMID 14490631.
- Webster GC, Varner JE (1955). "Aspartate metabolism and asparagine synthesis in plant systems". J. Biol. Chem. 215 (1): 91–99. doi:10.1016/S0021-9258(18)66019-3. PMID 14392145.
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