L-glutamate oxidase
| L-glutamate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.11 | ||||||||
| CAS no. | 39346-34-4 | ||||||||
| 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, L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are L-glutamic acid, water, and oxygen. Its products are α-ketoglutaric acid, hydrogen peroxide, and ammonia.[1][2]
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 L-glutamate:oxygen oxidoreductase (deaminating). Other names in common use include glutamate (acceptor) dehydrogenase, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor), and L-glutamic acid oxidase. It employs one cofactor, FAD.
References
- ^ Enzyme 1.4.3.11 at KEGG Pathway Database.
- ^ Yoshino H (1983). "Purification and properties of a new enzyme, L-glutamate oxidase, from Streptomyces sp X-119-6 grown on wheat bran". Agric. Biol. Chem. 47 (6): 1323–1328. doi:10.1271/bbb1961.47.1323.