In enzymology, an ureidosuccinase (EC 3.5.1.7) is an enzyme that catalyzes the chemical reaction
N-carbamoyl-L-aspartate + H2O ⇌ {\displaystyle \rightleftharpoons } L-aspartate + CO2 + NH3 Thus, the two substrates of this enzyme are N-carbamoyl-L-aspartate and H2O, whereas its 3 products are L-aspartate, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-L-aspartate amidohydrolase. This enzyme participates in alanine and aspartate metabolism.
References
LIEBERMAN I, KORNBERG A (1955). "Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III Ureidosuccinase". J. Biol. Chem. 212 (2): 909–20. doi:10.1016/S0021-9258(18)71029-6. PMID 14353892.
