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Ureidosuccinase

From Wikipedia, the free encyclopedia
ureidosuccinase
Identifiers
EC no.3.5.1.7
CAS no.9024-81-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

N-carbamoyl-L-aspartate + H2O 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

[edit]
  1. ^ "ureidosuccinase - Creative Biogene". www.microbialtec.com. Retrieved 2022-10-13.
  • LIEBERMAN I, KORNBERG A (1955). "Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III Ureidosuccinase". J. Biol. Chem. 212 (2): 909–20. PMID 14353892.