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Aspartate—ammonia ligase

From Wikipedia, the free encyclopedia
Aspartate—ammonia ligase
Identifiers
EC no.6.3.1.1
CAS no.9023-69-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 11AS and 12AS.

References

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  • 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.