Omega-amidase
| omega-amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.3 | ||||||||
| CAS number | 9025-19-8 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, an omega-amidase (EC 3.5.1.3) is an enzyme that catalyzes the chemical reaction
- a monoamide of a dicarboxylic acid + H2O a dicarboxylate + NH3
Thus, the two substrates of this enzyme are monoamide of a dicarboxylic acid and H2O, whereas its two products are dicarboxylate 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 omega-amidodicarboxylate amidohydrolase. This enzyme is also called alpha-keto acid-omega-amidase. This enzyme participates in glutamate metabolism and alanine and aspartate metabolism.
References
- MEISTER A, LEVINTOW L, GREENFIELD RE, ABENDSCHEIN PA (1955). "Hydrolysis and transfer reactions catalyzed by omega-amidase preparations". J. Biol. Chem. 215 (1): 441–60. PMID 14392177.
- Meister A, Radhakrishnan AN, Buckley SD (1957). "Enzymatic synthesis of L-pipecolic acid and L-proline". J. Biol. Chem. 229 (2): 789–800. PMID 13502341.
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