Biology:Ureidosuccinase

From HandWiki
Short description: Class of enzymes
ureidosuccinase
Identifiers
EC number3.5.1.7
CAS number9024-81-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, an ureidosuccinase (EC 3.5.1.7) is an enzyme that catalyzes the chemical reaction

N-carbamoyl-L-aspartate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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.[1]

References

  • "Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III Ureidosuccinase". J. Biol. Chem. 212 (2): 909–20. 1955. PMID 14353892.