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Information on EC 1.4.3.1 - D-aspartate oxidase
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1.4.3.1 D-aspartate oxidaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.4.3.1
-
d-amino
- n-methyl-d-aspartate
- nmda
- d-serine
- d-glutamate
-
nmdar-dependent
- octopus
-
flavoenzyme
- d-ser
- d-glu
-
d-amino-acid
-
prepulse
- d-alanine
- humicola
- molecular biology
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
aspartic oxidase, C47A10.5 gene product, C47Ap, ChDASPO, ChDDO, D-Asp oxidase, D-aspartic oxidase, D-AspO, DAO, DASOX, 
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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
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
D-aspartate:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9029-20-3
-
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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-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
-
-
?
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
-
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
-
-
-
?
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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-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
-
-
?
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
-
-
?
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-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
the enzyme shows high activity only with D-aspartate
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
391705, 391706, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 711719
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
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
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
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-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
preferred substrate
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
not influenced by Na+, K+, Mg2+, Ca2+, Co2+, Mn2+, and Zn2+
additional information
-
not influenced by Na+, K+, Mg2+, Ca2+, Co2+, Mn2+, and Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
-
i.e. thiolactomycin, active site-directed DDO inhibitor, competitive inhibition, competes with both the substrate and the coenzyme FAD; i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
-
i.e. thiolactomycin, active site-directed DDO inhibitor involving binding via Arg237, mixed type of inhibition, competes with both the substrate and the coenzyme FAD, structural models of mouse DDO/TLM complexes; i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD
additional information
not inhibited by EDTA, ATP, ADP, AMP, cAMP, and L-Asp
-
additional information
-
not inhibited by EDTA, ATP, ADP, AMP, cAMP, and L-Asp
-
additional information
not inhibited by clozapine, chlorpromazine, haloperidol, bupropion, fluoxetine, and amitriptyline
-
additional information
-
not inhibited by clozapine, chlorpromazine, haloperidol, bupropion, fluoxetine, and amitriptyline
-
additional information
not inhibited by clozapine, chlorpromazine, haloperidol, bupropion, fluoxetine, and amitriptyline
-
additional information
not inhibited by 10 mM meso-tartrate, benzoate, anthranilate, and crotonate
-
additional information
-
not inhibited by 10 mM meso-tartrate, benzoate, anthranilate, and crotonate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Aspartate
substrate activation at D-aspartate concentrations above 0.2 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dyskinesias
Higher free D-aspartate and N-methyl-D-aspartate levels prevent striatal depotentiation and anticipate L-DOPA-induced dyskinesia.
Zellweger Syndrome
The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
2.02
D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
1.2
D-Aspartate
mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
1.78
D-Aspartate
mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
2.37
D-Aspartate
His-tagged mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
4.87
D-Aspartate
wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
5.5
D-Aspartate
-
pH not specified in the publication, temperature not specified in the publication
7.3
D-Aspartate
His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
7.5
D-Aspartate
-
pH not specified in the publication, temperature not specified in the publication
7.63
D-Aspartate
mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
0.23
D-glutamate
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
0.25
D-glutamate
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
0.84
N-methyl-D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
1.84
N-methyl-D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
1.95
N-Methyl-D-aspartate
mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
2.67
N-Methyl-D-aspartate
His-tagged mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
4.23
N-Methyl-D-aspartate
mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
6.59
N-Methyl-D-aspartate
wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
7.81
N-Methyl-D-aspartate
mutant enzyme S308Y fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
8.02
N-Methyl-D-aspartate
His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
D-AspO kinetics in different tissues, overview
-
additional information
additional information
-
kinetics in comparison to the human DDO, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.07
D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
4.29
D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
2.11
D-glutamate
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
5.31
D-glutamate
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
3
N-methyl-D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
6.13
N-methyl-D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.66
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
-
pH 8.3, 37°C
0.0151
7-hydroxy-4-hydro-1,2,4-triazolo[4,3-a]pyrimidine-6-carboxylic acid
at pH 8.3 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.86
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
Mus musculus
-
pH 8.3, 37°C
1
1-hydroxy-1H-indole-2-carboxylic acid
Homo sapiens
IC50 above 1 mM, at pH 8.3 and 37°C
0.1
2-aminopyridine-4-carboxylic acid
Homo sapiens
IC50 above 0.1 mM, at pH 8.3 and 37°C
10
2-hydroxy-6-methylpyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
3-hydroxypyridine-2-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
0.1
4-aminopyridine-2-carboxylic acid
Homo sapiens
IC50 above 0.1 mM, at pH 8.3 and 37°C
0.1
4-aminopyridine-3-carboxylic acid
Homo sapiens
IC50 above 0.1 mM, at pH 8.3 and 37°C
5
4-carbamoylthiophene-2-carboxylic acid
Homo sapiens
IC50 above 5 mM, at pH 8.3 and 37°C
1
5-(dimethylamino)pyridine-3-carboxylic acid
Homo sapiens
IC50 above 1 mM, at pH 8.3 and 37°C
10
5-(trifluoromethyl)pyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
5-aminopyridine-2-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
5-bromopyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
5-chloropyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
5-fluoropyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
5-methoxypyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
10
5-nitropyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
5
5-phenylpyridine-3-carboxylic acid
Homo sapiens
IC50 above 5 mM, at pH 8.3 and 37°C
10
5-sulfopyridine-3-carboxylic acid
Homo sapiens
IC50 above 10 mM, at pH 8.3 and 37°C
0.1
6-aminopyridine-2-carboxylic acid
Homo sapiens
IC50 above 0.1 mM, at pH 8.3 and 37°C
0.0014
olanzapine
Mus musculus
in the presence of 0.004 mM FAD, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00119
0.04
0.09
pH 7.0, 20°C, purified recombinant mutant R243A, substrate D-Asp
0.1
wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.11
mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.24
mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.5
pH 7.0, 20°C, purified recombinant mutant R243K, substrate D-Glu
0.55
mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
1.2
pH 7.0, 20°C, purified recombinant mutant R243D, substrate N-methyl-D-Asp
1.5
pH 7.0, 20°C, purified recombinant mutant R243K, substrate D-Asp
1.6
pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Glu
1.9
pH 7.0, 20°C, purified recombinant mutant R243E, substrate D-Asp
13.1
18.5
pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Glu
181
pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Asp
2.37
mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
2.54
mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
4.31
wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
4.32
wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
5.55
mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
5.92
mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
9.2
pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate N-methyl-D-Asp
9.24
mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
93.7
pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Asp
additional information
mutant activities with D-Ala and D-Arg, overview
0.04
pH 7.0, 20°C, purified recombinant mutant R243E, substrate N-methyl-D-Asp
0.04
pH 7.0, 20°C, purified recombinant mutant R243K, substrate N-methyl-D-Asp
13.1
mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
13.1
pH 7.0, 20°C, purified recombinant mutant R243M, substrate D-Glu
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.3
additional information
-
optimum depends on the order of addition of the reactands
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 12.5
the activity increases gradually as the pH is increased from 6.0 to 8.3, remains approximately constant at pH 8.3 to 12.5, and decreases rapidly when the pH is greater than 12.5. No enzymatic activity is detected at very low and high pH levels (5.0 and 13.0), respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
391705, 391706, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 711719
-
-
brenda
at least three genes encoding functional DDO isozymes DDO-1, DDO-2, and DDO-3
-
-
brenda
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
-
-
brenda
gene C47Ap encoding isozyme DDO-1, gene F18Ep encoding isozyme DDO-2, and gene F20Hp encoding isozyme DDO-3
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
relatively high enzyme expression just after birth, the content gradually decreases thereafter
brenda