Biology:L-aspartate oxidase

From HandWiki
L-aspartate oxidase
Identifiers
EC number1.4.3.16
CAS number69106-47-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reaction

L-aspartate + H2O + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 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.

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

  • "L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase". J. Biol. Chem. 257 (2): 626–32. 1982. PMID 7033218.