1.4.3.1: D-aspartate oxidase
This is an abbreviated version!
For detailed information about D-aspartate oxidase, go to the full flat file.
Word Map on EC 1.4.3.1
-
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
- 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
Reaction
Synonyms
aspartic oxidase, C47A10.5 gene product, C47Ap, ChDASPO, ChDDO, D-Asp oxidase, D-aspartic oxidase, D-AspO, DAO, DASOX, DASPO, DDO, DDO-1, DDO-2, DDO-3, DDO1, DDO3, F18E3.7a gene product, F18Ep
ECTree
1.4.3.1 D-aspartate oxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.4.3.1 - D-aspartate oxidase
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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
-
-
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
preferred substrate
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
preferred substrate
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
activity is 2.5fold higher than with D-Asp, F18E3.7a gene product
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
activity is 67% of the activity with D-Asp, C47A10.5 gene product
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + 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-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
C47Ap exhibits 247% activity and F18Ep exhibits 67% activity compared to D-aspartate as substrate
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
preferred substrate. It is possible that excess amounts of D-Glu are as toxic for Caenorhabditis elegans as they are for the silkworm, and that Caenorhabditis elegans needs DDOs to deaminate D-Glu and thereby neutralize the toxicity of diet-derived D-Glu
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
14% activity compared to D-aspartate
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
ferricyanide and 2,6-dichlorophenolindophenol can also act as electron acceptors instead of O2
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
low activity
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
low activity
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
?
D-homocysteic acid + H2O + O2
2-oxo-4-sulfo-butanoate + NH3 + H2O2
-
-
-
-
?
D-homocysteic acid + H2O + O2
2-oxo-4-sulfo-butanoate + NH3 + H2O2
-
-
-
-
?
N-acetyl-DL-aspartate + H2O + O2
oxaloacetate + acetylamine + H2O2
-
-
-
-
?
N-acetyl-DL-aspartate + H2O + O2
oxaloacetate + acetylamine + H2O2
-
-
-
-
?
N-methyl-D-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
high activity
-
-
?
N-methyl-D-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
high activity
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
activity is 1.1fold higher than with D-Asp, C47A10.5 gene product
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
activity is 3.1fold higher than with D-Asp, F18E3.7a gene product
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
C47Ap exhibits 313% activity and F18Ep exhibits 110% activity compared to D-aspartate as substrate
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
83% activity compared to D-aspartate
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
Thermomyces dupontii NBRC 30541
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-Glu + H2O + O2
2-oxoglutarate + methylamine + H2O2
low activity
-
-
?
N-methyl-D-Glu + H2O + O2
2-oxoglutarate + methylamine + H2O2
low activity
-
-
?
N-methyl-L-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
low activity
-
-
?
N-methyl-L-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
low activity
-
-
?
additional information
?
-
-
chemical modification with phenylglyoxal results in irreversible loss of activity towards dicarboxylic D-amino acids, paralleled with a transient appearance of activity versus monocarboxylic ones
-
-
?
additional information
?
-
-
chemical modification with phenylglyoxal results in irreversible loss of activity towards dicarboxylic D-amino acids, paralleled with a transient appearance of activity versus monocarboxylic ones
-
-
?
additional information
?
-
-
chemical modification with phenylglyoxal results in irreversible loss of activity towards dicarboxylic D-amino acids, paralleled with a transient appearance of activity versus monocarboxylic ones
-
-
?
additional information
?
-
-
no detectable activity with L-alanine, L-methionine, and L-arginine
-
-
?
additional information
?
-
-
H2O2 that is generated in the enzymatic reaction catalyzed by Caenorhabditis elegans DDO-1 and DDO-2 is conceivably degraded by catalase colocalized with each DDO
-
-
?
additional information
?
-
-
all Caenorhabditis elegans DDOs exhibit the highest catalytic efficiency for D-Glu, but their efficiencies differ considerably for D-Glu, D-Asp, and NMDA. The isozymes show only very low or undetectable levels of activity against the neutral and basic D-amino acids and no activity with L-amino acids and N-methyl-L-Asp
-
-
?
additional information
?
-
-
in contrast to the mammalian and Cryptococcus humicola DDOs, the three kinds of Caenorhabditis elegans DDOs show relatively higher catalytic efficiency against D-Glu than against D-Asp and NMDA
-
-
?
additional information
?
-
no substrates: D-Asn, D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Pro, D-Phe, D-Met, D-Trp, D-Cys, D-Lys, D-Arg, D-His, L-Asp, L-Glu, LAsn, L-Gln, L-Ser, L-Thr, L-Tyr, L-Ala, L-Val, L-Leu, L-Ile, L-Pro, L-Phe, L-Met, L-Trp, L-Cys, L-Lys, L-Arg, L-His, and Gly
-
-
-
additional information
?
-
-
no substrates: D-Asn, D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Pro, D-Phe, D-Met, D-Trp, D-Cys, D-Lys, D-Arg, D-His, L-Asp, L-Glu, LAsn, L-Gln, L-Ser, L-Thr, L-Tyr, L-Ala, L-Val, L-Leu, L-Ile, L-Pro, L-Phe, L-Met, L-Trp, L-Cys, L-Lys, L-Arg, L-His, and Gly
-
-
-
additional information
?
-
-
structure-function relationships of DDO, overview
-
-
?
additional information
?
-
the enzyme exhibits low activities towards D-Glu and N-methyl-D-Glu, D-Asn, D-Pro and D-His. There is no activity detected towards D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Phe, D-Met, D-Trp, D-cysteine, D-Lys, D-Arg, L-Asp, L-Glu, N-methyl-L-Glu, L-Asn, L-Gln, L-Ser, L-Thr, L-Tyr, L-Ala, L-Val, L-Leu, L-Ile, L-Pro, L-Phe, L-Met, L-Trp, L-cysteine, L-Lys, L-Arg, L-His, or Gly
-
-
?
additional information
?
-
-
the enzyme exhibits low activities towards D-Glu and N-methyl-D-Glu, D-Asn, D-Pro and D-His. There is no activity detected towards D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Phe, D-Met, D-Trp, D-cysteine, D-Lys, D-Arg, L-Asp, L-Glu, N-methyl-L-Glu, L-Asn, L-Gln, L-Ser, L-Thr, L-Tyr, L-Ala, L-Val, L-Leu, L-Ile, L-Pro, L-Phe, L-Met, L-Trp, L-cysteine, L-Lys, L-Arg, L-His, or Gly
-
-
?
additional information
?
-
-
D-alanine,D-proline and L-asparagine are no substrates
-
-
?
additional information
?
-
-
Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding, overview
-
-
?
additional information
?
-
-
structure-function relationships of DDO, overview
-
-
?
additional information
?
-
the enzyme exhibits no activity towards D-Gln, D-Ser, D-Thr, D-Ala, D-Val, D-Leu, D-Phe, D-Met, D-Trp, D-cysteine, D-Lys, D-Arg, L-Asp, L-Glu, L-Asn, L-Gln, L-Ser, L-Thr, L-Ala, L-Val, L-Leu, L-Phe, L-Met, L-Trp, L-cysteine, L-Lys, L-Arg, or L-His
-
-
?
additional information
?
-
-
the enzyme exhibits no activity towards D-Gln, D-Ser, D-Thr, D-Ala, D-Val, D-Leu, D-Phe, D-Met, D-Trp, D-cysteine, D-Lys, D-Arg, L-Asp, L-Glu, L-Asn, L-Gln, L-Ser, L-Thr, L-Ala, L-Val, L-Leu, L-Phe, L-Met, L-Trp, L-cysteine, L-Lys, L-Arg, or L-His
-
-
?
additional information
?
-
-
D-AspO activity linearly increases with increasing D-Asp incubation times
-
-
?
additional information
?
-
-
Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding
-
-
?
additional information
?
-
substrate specificities of wild-type and mutants DDOs, overview
-
-
?
additional information
?
-
no activity with D-Ala, D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Gln, D-Met, D-Phe, D-Tyr, D-Trp, D-Lys, D-His, D-Arg, and Gly
-
-
?
additional information
?
-
-
no activity with D-Ala, D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Gln, D-Met, D-Phe, D-Tyr, D-Trp, D-Lys, D-His, D-Arg, and Gly
-
-
?
