Ureidosuccinase

From Wikipedia, the free encyclopedia

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.

[edit] References

• IUBMB entry for 3.5.1.7
• BRENDA references for 3.5.1.7 (Recommended.)
• PubMed references for 3.5.1.7
• PubMed Central references for 3.5.1.7
• Google Scholar references for 3.5.1.7
• LIEBERMAN I, KORNBERG A (1955). "Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III Ureidosuccinase". J. Biol. Chem. 212: 909–20. PMID 14353892. 

[edit] External links

The CAS registry number for this enzyme class is 9024-81-1.

• IUBMB entry for 3.5.1.7

• KEGG entry for 3.5.1.7

• BRENDA entry for 3.5.1.7

• NiceZyme view of 3.5.1.7

• EC2PDB: PDB structures for 3.5.1.7

• PRIAM entry for 3.5.1.7

• PUMA2 entry for 3.5.1.7

• IntEnz: Integrated Enzyme entry for 3.5.1.7

• MetaCyc entry for 3.5.1.7

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0050386: ureidosuccinase

• AMIGO entry for GO code 0050386: ureidosuccinase