L-aspartate oxidase
| L-aspartate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.16 | ||||||||
| CAS no. | 69106-47-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-aspartic acid and oxygen. Its products are iminosuccinic acid and hydrogen peroxide.[1] In Escherichia coli another enzyme, quinolinate synthase, takes the product with dihydroxyacetone phosphate to form quinolinic acid but simple hydrolysis gives oxaloacetic acid.[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 L-aspartate:oxygen oxidoreductase (deaminating). This enzyme is part of the pathway for alanine metabolism and nicotinamide adenine dinucleotide biosynthesis. It employs one cofactor, flavin adenine dinucleotide.[1]
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1J5P, 1KNP, and 1KNR.
References
- ^ a b Enzyme 1.4.3.16 at KEGG Pathway Database.
- ^ Nasu S, Wicks FD, Gholson RK (1982). "L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase". J. Biol. Chem. 257 (2): 626–32. doi:10.1016/S0021-9258(19)68239-6. PMID 7033218.