L-aspartate oxidase

L-Aspartate Oxidase

L-aspartate oxidase

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

L-aspartate + H<sub>2</sub>O + O<sub>2</sub> <math>rightleftharpoons</math> oxaloacetate + NH<sub>3</sub> + H<sub>2</sub>O<sub>2</sub>

The 3 substrates of this enzyme are L-aspartate, H<sub>2</sub>O, and O<sub>2</sub>, whereas its 3 products are oxaloacetate, NH<sub>3</sub>, and H<sub>2</sub>O<sub>2</sub>.

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 , , and .


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