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Aspartate ammonia-lyase
・ Aspartate carbamoyltransferase
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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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Aspartate ammonia-lyase : ウィキペディア英語版
Aspartate ammonia-lyase

In enzymology, an aspartate ammonia-lyase () is an enzyme that catalyzes the chemical reaction
:L-aspartate \rightleftharpoons fumarate + NH3
Hence, this enzyme has one substrate, L-aspartate, and two products, fumarate and NH3.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate 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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