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Aspartate—ammonia ligase : ウィキペディア英語版 | Aspartate—ammonia ligase
In enzymology, an aspartate-ammonia ligase () 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==
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
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