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Description:
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 .
References
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