L-aspartate oxidase
From Wikipedia, the free encyclopedia
In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reaction
- L-aspartate + H2O + O2 oxaloacetate + NH3 + H2O2
The 3 substrates of this enzyme are L-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, 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 L-aspartate:oxygen oxidoreductase (deaminating). This enzyme participates in alanine and aspartate metabolism and nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.
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[edit] Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1J5P, 1KNP, and 1KNR.
[edit] References
- IUBMB entry for 1.4.3.16
- BRENDA references for 1.4.3.16 (Recommended.)
- PubMed references for 1.4.3.16
- PubMed Central references for 1.4.3.16
- Google Scholar references for 1.4.3.16
- 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: 626–32. PMID 7033218.
[edit] External links
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- The CAS registry number for this enzyme class is 69106-47-4.