L-amino-acid Oxidase

In enzymology, a L-amino-acid oxidase (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction

an L-amino acid + H2O + O2 a 2-oxo acid + NH4 + H2O2

The 3 substrates of this enzyme are L-amino acid, H2O, and O2, whereas its 3 products are the corresponding α-keto acid (2-oxo acid), NH4, and H2O2. For example, the enzyme will convert L-alanine into pyruvic acid (2-oxopropanoic acid).

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.

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