| ureidosuccinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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]
- ^ "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.
| ureidosuccinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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]
- ^ "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.