Ureidosuccinase
Class of enzymes From Wikipedia, the free encyclopedia
Class of enzymes From Wikipedia, the free encyclopedia
In enzymology, an ureidosuccinase (EC 3.5.1.7) is an enzyme that catalyzes the chemical reaction
ureidosuccinase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.7 | ||||||||
CAS no. | 9024-81-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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]
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