L-aspartate oxidase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 1.4.3.16 | ||||||||
CAS no. | 69106-47-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are L-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, 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-aspartate:oxygen oxidoreductase (deaminating). This enzyme participates in alanine and aspartate metabolism and nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1J5P, 1KNP, and 1KNR.
In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction
In enzymology, a glyoxylate oxidase (EC 1.2.3.5) is an enzyme that catalyzes the chemical reaction
In enzymology, an indole-3-acetaldehyde oxidase (EC 1.2.3.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a retinal oxidase (EC 1.2.3.11) is an enzyme that catalyzes the chemical reaction
Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
In enzymology, a cyclohexylamine oxidase (EC 1.4.3.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-aspartate oxidase (EC 1.4.3.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-glutamate(D-aspartate) oxidase (EC 1.4.3.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-glutamate oxidase (EC 1.4.3.7) is an enzyme that catalyzes the chemical reaction
In enzymology, an ethanolamine oxidase (EC 1.4.3.8) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-lysine 6-oxidase (EC 1.4.3.20) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-lysine oxidase (EC 1.4.3.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a methanethiol oxidase (EC 1.8.3.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a N6-methyl-lysine oxidase (EC 1.5.3.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a nitroalkane oxidase (EC 1.7.3.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a putrescine oxidase (EC 1.4.3.10) is an enzyme that catalyzes the chemical reaction
In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction
Glycine oxidase (EC 1.4.3.19) is an enzyme with systematic name glycine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction