aspartate ammonia-lyase

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as·par·tate am·mo·ni·a-ly·ase

a nonmammalian enzyme that catalyzes the conversion of l-aspartate to fumarate, splitting out ammonia.
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However, it has been shown that the kinetics of enzymes can be changed by polyhydric alcohols (25) and that aspartase is activated by glycerol, ethylene glycol (1,2-ethanediol), and propylene glycol (1,2-propanediol) (26).
Thirteen patients had mild serum elevations of liver enzymes aspartase aminotransferase, alanine aminotransferase, and lactate dehydrogenase.
Caspases (also known as cysteine-aspartic proteases, cysteine aspartases, or cysteine-dependent aspartate-directed proteases) are the family of intracellular proteases that cleave substrates in a highly specific manner after the Asp residue in short tetrapeptide (X-X-X-Asp) motifs [43].