Biology:D-glutamate oxidase
From HandWiki
| D-glutamate oxidase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.4.3.7 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a D-glutamate oxidase (EC 1.4.3.7) is an enzyme that catalyzes the chemical reaction
- D-glutamate + H2O + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2-oxoglutarate + NH3 + H2O2
The 3 substrates of this enzyme are D-glutamate, H2O, and O2, 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 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
- "Purification and properties of D-glutamic acid oxidase from Octopus vulgaris Lam". Arch. Biochem. Biophys. 77 (2): 336–49. 1958. 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. PMID 4387700.
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