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Enzyme Nomenclature
Information on EC 1.4.3.1 - D-aspartate oxidase
for references in articles please use BRENDA:EC1.4.3.1
Word Map on EC 1.4.3.1
- 1.4.3.1
-
d-amino
- n-methyl-d-aspartate
- d-glutamate
- beef
- d-serine
- octopus
-
nmdars
-
nmdar-dependent
- d-alanine
-
d-amino-acid
- d-glu
-
prepulse
- molecular biology
- drug development
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.4.3.1
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RECOMMENDED NAME
GeneOntology No.
D-aspartate oxidase
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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
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-
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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391705, 391706, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 711719
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; 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
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at least three genes encoding functional DDO isozymes DDO-1, DDO-2, and DDO-3
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gene C47Ap encoding isozyme DDO-1, gene F18Ep encoding isozyme DDO-2, and gene F20Hp encoding isozyme DDO-3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
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melatonin secretion and D-Asp release from pinealocytes are enhanced by stimulation with noradrenaline, after which the melatonin secretion is suppressed by the action of the released D-Asp on the cells. Through this negative feedback mechanism, noradrenaline may regulate its ability to induce melatonin secretion in the pineal gland
metabolism
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in frog tissue, D-AspO plays an essential role in modulating the D-Asp concentration, exaggerated D-Asp concentrations activate SOD1 as cytoprotective mechanism in the kidney, whereas, in the brain and in the heart, where the antioxidant action of SOD1 is limited, caspase 3 is activated, overview
metabolism
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H2O2 is essential for the iodination of the tyrosyl residues to produce mono- and diiodotyrosine that are the precursors for the synthesis of thyroid hormones T3 and T4. interaction of endogenous D-Asp, D-AspO, and D-aspartate racemase in thyroid gland constitutes an additional biochemical pathway for the production of H2O2 and consequently for the synthesis of thyroid hormones, overview
metabolism
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H2O2 is essential for the iodination of the tyrosyl residues to produce mono- and diiodotyrosine that are the precursors for the synthesis of thyroid hormones T3 and T4. interaction of endogenous D-Asp, D-AspO, and D-aspartate racemase in thyroid gland constitutes an additional biochemical pathway for the production of H2O2 and consequently for the synthesis of thyroid hormones, overview
physiological function
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D-Asp oxidase is a FAD-containing flavoprotein that catalyzes the oxidative deamination of D-amino acids with O2 to generate the corresponding 2-oxo acids, along with H2O2 and NH3. DDO is highly specific for acidic D-amino acids, such as D-Asp, N-methyl-D-Asp, and D-Glu
physiological function
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relevance of D-Asp and DDO to NMDA receptor-related disease, D-Asp protects against sensorimotor-gating deficits, which are observed in schizophrenic patients, overview. D-Asp is important in the development and neurogenesis of the brain
physiological function
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relevance of D-Asp and DDO to NMDA receptor-related disease, overview. Phenotype of DDO-deficient mice, DDO-deficient mice display significant deficits in prepulse inhibition, and exhibit reduced immobility time in the Porsolt forced-swim test, a model of depression, suggesting that the genetic ablation of DDO has a specific antidepressant action, overview
physiological function
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D-Asp is important in the development and neurogenesis of the brain. D-Asp plays a regulatory role in the synthesis and secretion of prolactin in the anterior lobe of the pituitary gland. D-Asp directly interacts with DNA and/or acts on nuclear protein(s) involved in the regulation of gene transcription, through which d-Asp controls gene expression in the hypothalamo-neurohypophyseal system
physiological function
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in frog tissue, D-AspO plays an essential role in modulating the D-Asp concentration. Induction of oxidative stress following D-Asp exposure is primarily related to its metabolism by inducible D-AspO
physiological function
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D-AspO plays an essential role in decreasing excessive amounts of D-Asp in frog tissues
physiological function
the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells; the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells; the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells
physiological function
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age-related changes in D-aspartate oxidase promoter methylation control extracellular D-aspartate levels and prevent precocious cell death during brain aging. The enzyme expression is critical to regulate the content of the N-methyl-D-aspartate receptor agonist D-aspartate in adulthood
physiological function
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the enzyme plays a role in the modulation of glutamatergic system homeostasis in the mammalian brain
physiological function
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the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells; the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells; the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells
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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
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-
?
D-aspartic acid-beta-hydroxamate + H2O + O2
4-(hydroxyamino)-2,4-dioxobutanoic acid + NH3 + H2O2
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-
-
-
?
D-Gln + H2O + O2
? + NH3 + H2O2
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substrate for mutant enzymes H56A and H56N
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-
?
D-Met + H2O + O2
4-(methylsulfonyl)-2-oxobutanoate + NH3 + H2O2
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substrate for mutant enzymes H56A and H56N
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?
D-methionine + H2O + O2
4-(methylsulfonyl)-2-oxobutanoic acid + NH3 + H2O2
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1.8% activity compared to D-aspartate
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-
?
D-methionine + H2O + O2
?
-
C47Ap exhibits 3.8% activity and F18Ep exhibits 2.4% activity compared to D-aspartate as substrate
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-
?
D-Phe + H2O + O2
? + NH3 + H2O2
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substrate for mutant enzymes H56A and H56N
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-
?
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
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-
?
L-glutamine + H2O + O2
?
-
C47Ap exhibits 1.3% activity and F18Ep exhibits 0.3% activity compared to D-aspartate as substrate
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-
?
N-methyl-L-asparagine + H2O + O2
?
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C47Ap exhibits 6.7% activity and F18Ep exhibits 1.1% activity compared to D-aspartate as substrate
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-
?
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
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-
-
?
D-alanine + H2O + O2
?
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C47Ap exhibits 4.5% activity and F18Ep exhibits 2.8% activity compared to D-aspartate as substrate
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-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
Q75WF1
arginine residue 243 is possibly involved in the substrate recognition, active site model, overview
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?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
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the enzyme shows high activity only with D-aspartate
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?
D-asparagine + H2O + O2
?
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C47Ap exhibits 17% activity and F18Ep exhibits 6.1% activity compared to D-aspartate as substrate
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-
?
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
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?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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-
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?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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100% activity
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?
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
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-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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-
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?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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-
-
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?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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this enzyme is proposed to have a role in the inactivation of the synaptically released D-aspartate
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?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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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
-
-
-
-
?
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
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-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
ferricyanide and 2,6-dichlorophenolindophenol can also act as electron acceptors instead of O2
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?
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
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?
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
Q75WF1
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
Q75WF1
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
O45307, Q19564
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
O45307, Q19564
-
-
-
?
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, 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
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
-
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.
INHIBITORS
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 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
-
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.
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
-
37°C, pH 8.3, C47A10.5 gene product; recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
0.25
D-glutamate
-
37°C, pH 8.3, F18E3.7a gene product; 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 in comparison to the human DDO, overview
-
additional information
additional information
-
D-AspO kinetics in different tissues, overview
-
additional information
additional information
Q75WF1
kinetics of wild-type and mutant enzymes, 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
-
37°C, pH 8.3, F18E3.7a gene product; recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
5.31
D-glutamate
-
37°C, pH 8.3, C47A10.5 gene product; 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
1117
D-Glu
-
pH 8.3, 37°C, recombinant DDO-3; pH 8.3, 37°C,recombinant DDO-3
3759
D-Glu
-
pH 8.3, 37°C, recombinant DDO-2; pH 8.3, 37°C,recombinant DDO-2
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
10
2-hydroxy-6-methylpyridine-3-carboxylic acid
Homo sapiens
-
IC50 above 10 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
0.0014
olanzapine
Mus musculus
-
in the presence of 0.004 mM FAD, pH and temperature not specified in the publication
0.0231
olanzapine
Homo sapiens
-
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
Q75WF1
pH 7.0, 20°C, purified recombinant mutant R243E, substrate N-methyl-D-Asp; pH 7.0, 20°C, purified recombinant mutant R243K, substrate N-methyl-D-Asp
0.09
Q75WF1
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
0.55
-
mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
1.2
Q75WF1
pH 7.0, 20°C, purified recombinant mutant R243D, substrate N-methyl-D-Asp
1.6
Q75WF1
pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Glu
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
Q75WF1
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
13.1
18.5
Q75WF1
pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Glu
93.7
Q75WF1
pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Asp
additional information
Q75WF1
mutant activities with D-Ala and D-Arg, overview
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
Q75WF1
pH 7.0, 20°C, purified recombinant mutant R243M, substrate D-Glu
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
relatively high enzyme expression just after birth, the content gradually decreases thereafter
additional information
-
embryonic, D-Asp initially emerges in the hindbrain and then spreads into the forebrain. Within nerve cells of the rat embryonic brain, D-Asp first occurs in the cell bodies of neuroblasts in the outer layer of the neuronal epithelium, and then it appears in the processes of the cells
-
relatively high enzyme expression just after birth, the content gradually decreases thereafter