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 $\rightleftharpoons$ 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.

[edit] Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1F8R, 1F8S, 1REO, 1TDK, 1TDN, 1TDO, 2IID, 2JAE, 2JB1, 2JB2, and 2JB3.

IUBMB entry for 1.4.3.2
BRENDA references for 1.4.3.2 (Recommended.)
PubMed references for 1.4.3.2
PubMed Central references for 1.4.3.2
Google Scholar references for 1.4.3.2
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 609-648.
Wellner D and Meister A (1960). "Crystalline L-amino acid oxidase of Crotalus adamanteus". J. Biol. Chem. 235: 2013–2018.