| carboxymethylhydantoinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.2.4 | ||||||||
| CAS no. | 9025-14-3 | ||||||||
| 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, a carboxymethylhydantoinase (EC 3.5.2.4) is an enzyme that catalyzes the chemical reaction
- L-5-carboxymethylhydantoin + H2O N-carbamoyl-L-aspartate
N-carbamoyl-L-aspartateThus, the two substrates of this enzyme are L-5-carboxymethylhydantoin and H2O, whereas its product is N-carbamoyl-L-aspartate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is L-5-carboxymethylhydantoin amidohydrolase. This enzyme is also called hydantoin hydrolase.
References
- LIEBERMAN I, KORNBERG A (1954). "Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. I Dihydroortic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin". J. Biol. Chem. 207 (2): 911–24. PMID 13163076.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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