D-aspartate oxidase
| D-aspartate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.4.3.1 | ||||||||
| CAS number | 9029-20-3 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a D-aspartate oxidase (EC 1.4.3.1) is an enzyme that catalyzes the chemical reaction
- D-aspartate + H2O + O2 oxaloacetate + NH3 + H2O2
The 3 substrates of this enzyme are D-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2.
This enzyme belongs to the FAD dependent oxidoreductase family, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-aspartate:oxygen oxidoreductase (deaminating). Other names in common use include aspartic oxidase, and D-aspartic oxidase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, FAD.
The enzyme is encoded by DDO gene.
References
- Dixon M, Kenworthy P (1967). "D-aspartate oxidase of kidney". Biochim. Biophys. Acta. 146 (1): 54–76. doi:10.1016/0005-2744(67)90073-3. PMID 6060479.
- Still JL, Buell MV, Knox WE, Green DE (1949). "Studies on the cyclophorase system. VII. D-Aspartic oxidase". J. Biol. Chem. 179: 831–837.
- Still JL; Sperling E (1950). "On the prosthetic group of the D-aspartic oxidase". J. Biol. Chem. 182: 585–589.
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