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・ Aspartame
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・ Aspartate 4-decarboxylase
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Aspartate—ammonia ligase
・ Aspartate—ammonia ligase (ADP-forming)
・ Aspartate—phenylpyruvate transaminase
・ Aspartate—prephenate aminotransferase
・ Aspartate—tRNA ligase
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・ Aspartic alpha-decarboxylase
・ Aspartoacylase
・ Aspartyl aminopeptidase
・ Aspartylglucosamine
・ Aspartylglucosaminidase
・ Aspartylglucosaminuria
・ Aspartyltransferase


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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 \rightleftharpoons 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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