D-glutamate(D-aspartate) oxidase
| D-glutamate(D-aspartate) oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.15 | ||||||||
| 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(D-aspartate) oxidase (EC 1.4.3.15) 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. The enzyme can also act in a similar way on D-aspartic acid.[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 D-glutamate(D-aspartate):oxygen oxidoreductase (deaminating). Other names in common use include D-glutamic-aspartic oxidase, and D-monoaminodicarboxylic acid oxidase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, flavin adenine dinucleotide.[1]
References
- ^ a b Enzyme 1.4.3.15 at KEGG Pathway Database.
- ^ Mizushima S (1957). "Purified D-glutamic-aspartic oxidase of Aspergillus ustus". J. Gen. Appl. Microbiol. 3: 233–239. doi:10.2323/jgam.3.233.