D-glutamate oxidase
| D-glutamate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.7 | ||||||||
| CAS no. | 37255-41-7 | ||||||||
| 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, D-glutamate oxidase (EC 1.4.3.7) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are D-glutamic acid, water, and oxygen. Its products are α-ketoglutaric acid, hydrogen peroxide, and ammonia.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-glutamate:oxygen oxidoreductase (deaminating). Other names in common use include D-glutamic oxidase, and D-glutamic acid oxidase. This enzyme participates in d-glutamine and d-glutamate metabolism.
References
- ^ Enzyme 1.4.3.7 at KEGG Pathway Database.
- ^ Rocca E, Ghiretti F (1958). "Purification and properties of D-glutamic acid oxidase from Octopus vulgaris Lam". Arch. Biochem. Biophys. 77 (2): 336–49. doi:10.1016/0003-9861(58)90081-X. PMID 13583997.
- ^ Urich K (1968). "[D-Glutamate oxidase from the antennal gland of the crayfish Oronectes limosus: purification and characterization]". Z. Naturforsch. B. 23 (11): 1508–11. doi:10.1515/znb-1968-1114. PMID 4387700.