D-aspartate oxidase
| D-aspartate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.1 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
In enzymology, D-aspartate oxidase (EC 1.4.3.1) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are D-aspartic acid, water and oxygen. Its products are oxaloacetic acid, hydrogen peroxide, and ammonia.[1][2][3][4]
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.[5]
See also
References
- ^ Enzyme 1.4.3.1 at KEGG Pathway Database.
- ^ Still JL, Buell MV, Knox WE, Green DE (1949). "Studies on the cyclophorase system. VII. D-Aspartic oxidase". J. Biol. Chem. 179 (2): 831–837. doi:10.1016/S0021-9258(19)51276-5.
- ^ Still JL; Sperling E (1950). "On the prosthetic group of the D-aspartic oxidase". J. Biol. Chem. 182 (2): 585–589. doi:10.1016/S0021-9258(18)56492-9.
- ^ 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.
- ^ Setoyama C, Miura R (Jul 1997). "Structural and functional characterization of the human brain D-aspartate oxidase". J Biochem. 121 (4): 798–803. doi:10.1093/oxfordjournals.jbchem.a021655. PMID 9163533.