In enzymology, an aspartate—ammonia ligase (EC 6.3.1.1) is an enzyme that catalyzes the chemical reaction
| Aspartate—ammonia ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.1 | ||||||||
| CAS no. | 9023-69-2 | ||||||||
| 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 | ||||||||
| |||||||||
- 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 11AS and 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: 2845–9. PMID 14490631.
- Webster GC, Varner JE (1955). "Aspartate metabolism and asparagine synthesis in plant systems". J. Biol. Chem. 215: 91–99. PMID 14392145.
