Any feedback?
Information on EC 1.4.3.1 - D-aspartate oxidase
for references in articles please use BRENDA:EC1.4.3.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.4.3.1 D-aspartate oxidaseIUBMB Comments
A flavoprotein (FAD).
Specify your search results
Word Map
- 1.4.3.1
-
d-amino
- n-methyl-d-aspartate
- nmda
- d-serine
- d-glutamate
- octopus
-
nmdar-dependent
- d-alanine
-
prepulse
- humicola
-
d-amino-acid
- d-ser
- d-glu
- drug development
- molecular biology
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-aspartate oxidase, daspo, d-aspo, ddo-3, chddo, ddo-1, f18ep, c47ap, d-asp oxidase, chdaspo, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspartic oxidase
-
-
-
-
C47Ap
D-Asp oxidase
D-aspartic oxidase
-
-
-
-
D-AspO
DAO
DASOX
-
-
-
-
DASPO
DDO
DDO-1
DDO-2
DDO-3
F18Ep
C47Ap
-
the protein with DASPO activity shows distinct kinetic properties against D-Asp, D-Glu, and N-methyl-D-Asp
F18Ep
-
the protein with DASPO activity shows distinct kinetic properties against D-Asp, D-Glu, and N-methyl-D-Asp
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-aspartate:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9029-20-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 meso-2,3-diaminosuccinate + O2
pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3
D-arginine + H2O + O2
?
-
C47Ap exhibit less than 0.1% activity compared to D-aspartate as substrate
-
-
?
D-Asn + H2O + O2
? + NH3 + H2O2
substrate for mutant enzyme H56N
-
-
?
D-aspartic acid-beta-hydroxamate + H2O + O2
4-(hydroxyamino)-2,4-dioxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-Gln + H2O + O2
? + NH3 + H2O2
substrate for mutant enzymes H56A and H56N
-
-
?
D-Leu + H2O + O2
? + NH3 + H2O2
substrate for mutant enzyme H56N
-
-
?
D-Met + H2O + O2
4-(methylsulfonyl)-2-oxobutanoate + NH3 + H2O2
substrate for mutant enzymes H56A and H56N
-
-
?
D-methionine + H2O + O2
4-(methylsulfonyl)-2-oxobutanoic acid + NH3 + H2O2
-
1.8% activity compared to D-aspartate
-
-
?
D-methionine + H2O + O2
?
-
C47Ap exhibits 3.8% activity and F18Ep exhibits 2.4% activity compared to D-aspartate as substrate
-
-
?
D-Phe + H2O + O2
? + NH3 + H2O2
substrate for mutant enzymes H56A and H56N
-
-
?
D-thiazolidine-2-carboxylate + H2O + O2
(ethylthio)oxoacetic acid + H2O2 + NH3
-
-
-
-
?
DL-2-amino-3-phosphonopropanoic acid + H2O + O2
2-oxo-3-phosphonopropanoic acid + NH3 + H2O2
-
-
-
-
?
L-asparagine + H2O + O2
?
-
C47Ap exhibits 2.6% activity and F18Ep exhibits less than 0.1% activity compared to D-aspartate as substrate
-
-
?
L-glutamine + H2O + O2
?
-
C47Ap exhibits 1.3% activity and F18Ep exhibits 0.3% activity compared to D-aspartate as substrate
-
-
?
N-methyl-L-asparagine + H2O + O2
?
-
C47Ap exhibits 6.7% activity and F18Ep exhibits 1.1% activity compared to D-aspartate as substrate
-
-
?
3 meso-2,3-diaminosuccinate + O2
pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3
-
-
-
?
3 meso-2,3-diaminosuccinate + O2
pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3
-
-
-
?
3 meso-2,3-diaminosuccinate + O2
pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3
-
-
-
?
3 meso-2,3-diaminosuccinate + O2
pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3
-
-
-
?
3 meso-2,3-diaminosuccinate + O2
pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3
-
-
-
?
D-alanine + H2O + O2
?
-
C47Ap exhibits 4.5% activity and F18Ep exhibits 2.8% activity compared to D-aspartate as substrate
-
-
?
D-Asn + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
low activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
arginine residue 243 is possibly involved in the substrate recognition, active site model, overview
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
the enzyme shows high activity only with D-aspartate
-
-
?
D-asparagine + H2O + O2
?
-
C47Ap exhibits 17% activity and F18Ep exhibits 6.1% activity compared to D-aspartate as substrate
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
100% activity
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
this enzyme is proposed to have a role in the inactivation of the synaptically released D-aspartate
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
ferricyanide and 2,6-dichlorophenolindophenol can also act as electron acceptors instead of O2
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
DASPO plays an essential role in the assimilation of D-aspartate and acts as a detoxifying agent for D-aspartate. In the wild-type strain, the induction of ChDASPO activity strictly depends on the presence of D-aspartate and is little affected by the copresence of ammonium chloride, but it is significantly reduced by the copresence of both glucose and ammonium chloride, which, however, did not abolish the induction, allowing considerable expression of ChDASPO
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
intermediate product is iminoaspartate
-
?
D-aspartate dimethylester + H2O + O2
oxaloacetic acid dimethylester + H2O2 + NH3
-
-
-
-
?
D-aspartate dimethylester + H2O + O2
oxaloacetic acid dimethylester + H2O2 + NH3
-
-
-
-
?