| 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 | ||||||||
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In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reaction
- L-glutamate + O2 + H2O 2-oxoglutarate + NH3 + H2O2
2-oxoglutarate + NH3 + H2O2The 3 substrates of this enzyme are L-glutamate, O2, and H2O, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2.
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
- 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.
| CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1: NAD/NADP acceptor | |
| 1.4.3: oxygen acceptor | |
| 1.4.4: disulfide acceptor | |
| 1.4.99: other acceptors | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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