L-amino-acid oxidase

In enzymology, a L-amino-acid oxidase is an enzyme that catalyzes the chemical reaction


 * an L-amino acid + H2O + O2 $$\rightleftharpoons$$ a 2-oxo acid + NH3 + H2O2

The 3 substrates of this enzyme are L-amino acid, H2O, and O2, whereas its 3 products are 2-oxo acid, 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-amino-acid:oxygen oxidoreductase (deaminating). This enzyme is also called ophio-amino-acid oxidase. This enzyme participates in 8 metabolic pathways: alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis. It employs one cofactor, FAD.

Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , and.