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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
cis-2,3-piperidine dicarboxylic acid + H2O + O2
?
-
-
-
-
?
cis-2,3-piperidinedicarboxylate + H2O + O2
?
D-alpha-aminoadipic acid + H2O + O2
2-oxoadipic acid + NH3 + H2O2
-
-
-
-
?
D-aminoadipate + H2O + O2
?
D-arginine + H2O + O2
?
-
C47Ap exhibit less than 0.1% activity compared to D-aspartate as substrate
-
-
?
D-Asn + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
D-Asn + H2O + O2
? + NH3 + H2O2
substrate for mutant enzyme H56N
-
-
?
D-Asn + H2O + O2
oxaloacetate + NH3 + H2O2
low activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
D-asparagine + H2O + O2
2-oxosuccinamic acid + H2O2 + NH3
D-asparagine + H2O + O2
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
D-aspartate dimethylester + H2O + O2
oxaloacetic acid dimethylester + H2O2 + NH3
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-Glu + H2O + O2
2-oxoglutarate + H2O2 + NH3
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
D-glutamine + H2O + O2
2-oxoglutaric acid + H2O2 + NH3
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
D-homocysteic acid + H2O + O2
2-oxo-4-mercapto-butanoate
D-homocysteic acid + H2O + O2
2-oxo-4-sulfobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-hydroxyglutarate + H2O + O2
?
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-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
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
-
-
-
-
?
DL-cysteic acid + H2O + O2
2-oxo-3-sulfopropionic acid + NH3 + H2O2
-
-
-
-
?
glycyl-D-aspartic acid + H2O + O2
?
-
-
-
-
?
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
-
-
?
meso-2,3-diaminosuccinate + H2O + O2
?
N-acetyl-DL-aspartate + H2O + O2
oxaloacetate + acetylamine + H2O2
N-methyl-D-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
N-methyl-D-asparagine + H2O + O2
?
-
-
-
-
r
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
N-methyl-D-Glu + H2O + O2
2-oxoglutarate + methylamine + H2O2
N-methyl-L-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
N-methyl-L-asparagine + H2O + O2
?
-
C47Ap exhibits 6.7% activity and F18Ep exhibits 1.1% activity compared to D-aspartate as substrate
-
-
?
N-methyl-L-aspartate + H2O + O2
?
-
4% activity compared to D-aspartate
-
-
?
additional information
?
-
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
-
-
-
?
cis-2,3-piperidinedicarboxylate + H2O + O2

?
-
-
-
-
?
cis-2,3-piperidinedicarboxylate + H2O + O2
?
-
-
-
-
?
D-alanine + H2O + O2

?
-
C47Ap exhibits 4.5% activity and F18Ep exhibits 2.8% activity compared to D-aspartate as substrate
-
-
?
D-alanine + H2O + O2
?
-
low catalytic efficiency with D-alanine
-
-
?
D-aminoadipate + H2O + O2

?
-
-
-
-
?
D-aminoadipate + H2O + O2
?
-
-
-
-
?
D-Asn + H2O + O2

2-oxosuccinamic acid + NH3 + H2O2
low activity
-
-
?
D-Asn + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
low activity
-
-
?
D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
high activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
high activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
high activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
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

2-oxosuccinamic acid + H2O2 + NH3
-
-
-
-
r
D-asparagine + H2O + O2
2-oxosuccinamic acid + H2O2 + NH3
-
-
-
-
?
D-asparagine + H2O + O2

?
-
C47Ap exhibits 17% activity and F18Ep exhibits 6.1% activity compared to D-aspartate as substrate
-
-
?
D-asparagine + H2O + O2
?
-
15% activity compared to 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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
-
?
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
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
100% activity
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
ferricyanide and 2,6-dichlorophenolindophenol can also act as electron acceptors instead of O2
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
-
?
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
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
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 + H2O2 + NH3
low activity
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + H2O2 + NH3
low activity
-
-
?
D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2
-
preferred substrate
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
low activity
-
-
?
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
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
14% activity compared to D-aspartate
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
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-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2

2-oxoglutaric acid + H2O2 + NH3
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaric acid + H2O2 + NH3
-
-
-
-
?
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-homocysteic acid + H2O + O2

2-oxo-4-mercapto-butanoate
-
-
-
-
?
D-homocysteic acid + H2O + O2
2-oxo-4-mercapto-butanoate
-
-
-
-
?
D-hydroxyglutarate + H2O + O2

?
-
-
-
-
?
D-hydroxyglutarate + H2O + O2
?
-
-
-
-
?
D-Pro + H2O + O2

2-oxopentanoic acid + NH3 + H2O2
low activity
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
low activity
-
-
?
D-proline + H2O + O2

2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
meso-2,3-diaminosuccinate + H2O + O2

?
-
-
-
-
?
meso-2,3-diaminosuccinate + H2O + O2
?
-
-
-
-
?
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
-
-
-
-
?
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-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-Asp + H2O + O2
oxaloacetate + methylamine + 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 + 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
-
-
-
?
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 + 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-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
-
-
?
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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
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
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
-
-
?
N-methyl-D-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
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
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
high activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
high activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
high activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
intermediate product is iminoaspartate
-
-
?
D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2
-
preferred substrate
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-Asp + 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-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
-
?
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4.5
cis-2,3-piperidine dicarboxylic acid
-
-
742
D-alanine
-
pH and temperature not specified in the publication
16.2
D-alpha-aminoadipic acid
-
-
83.4
D-Asn
mutant enzyme H56N, at pH 7.5 and 37ưC
150 - 540
D-aspartate dimethylester
3
D-aspartic acid-beta-hydroxamate
-
-
9.8
D-homocysteic acid
-
-
8.8
D-Leu
mutant enzyme H56N, at pH 7.5 and 37ưC
15.2
DL-2-amino-3-phosphonopropanoic acid
-
-
143
glycyl-D-aspartic acid
-
-
4.8
meso-2,3-Diaminosuccinate
-
-
2.85 - 27.9
N-methyl-D-Asp
0.84 - 1.84
N-methyl-D-asparagine
0.2 - 85.3
N-Methyl-D-aspartate
additional information
additional information
-
1
D-Asp

pH 7.0, 20ưC, recombinant mutant R243D
2
D-Asp
pH 7.0, 20ưC, recombinant mutant R243E
2.1
D-Asp
at pH 8.3 and 37ưC
2.26
D-Asp
at pH 8.3 and 37ưC
2.5
D-Asp
wild type enzyme, at pH 7.5 and 37ưC
2.5
D-Asp
pH 7.0, 20ưC, recombinant wild-type enzyme
3.8
D-Asp
pH 7.0, 20ưC, recombinant mutant R243M
3.81
D-Asp
-
pH 8.3, 37ưC, recombinant DDO-3
4.2
D-Asp
-
pH 8.3, 37ưC, recombinant DDO-2
4.22
D-Asp
-
pH 8.2, 37ưC, kidney
4.26
D-Asp
-
pH 8.2, 37ưC, brain
4.41
D-Asp
-
pH 8.2, 37ưC, liver
5.54
D-Asp
-
pH 8.3, 37ưC, recombinant DDO-1
7.37
D-Asp
at pH 8.3 and 37ưC
10.3
D-Asp
pH 7.0, 20ưC, recombinant mutant R243K
13.4
D-Asp
pH 7.0, 20ưC, recombinant mutant R243A
0.38
D-asparagine

-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37ưC
2.02
D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37ưC
0.38
D-Aspartate

-
37ưC, pH 8.3, F18E3.7a gene product
0.86
D-Aspartate
-
O2 as acceptor
1.2
D-Aspartate
mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
1.3
D-Aspartate
-
pH and temperature not specified in the publication
1.6
D-Aspartate
-
at 25ưC
1.78
D-Aspartate
mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
2.02
D-Aspartate
-
37ưC, pH 8.3, C47A10.5 gene product
2.2
D-Aspartate
-
at 4ưC
2.37
D-Aspartate
His-tagged mutant enzyme S308G, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
2.5
D-Aspartate
-
at pH 8.3
2.9
D-Aspartate
37ưC, pH 7.5
4.87
D-Aspartate
wild type enzyme fused N-terminally with glutathione S-transferase, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
5.2
D-Aspartate
-
ferricyanide as acceptor
5.5
D-Aspartate
-
pH not specified in the publication, temperature not specified in the publication
5.7
D-Aspartate
-
at pH 7.4
7.3
D-Aspartate
His-tagged wild type enzyme, at 37ưC 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 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
150
D-aspartate dimethylester

-
-
540
D-aspartate dimethylester
-
-
21
D-Gln

mutant enzyme H56N, at pH 7.5 and 37ưC
39.4
D-Gln
mutant enzyme H56A, at pH 7.5 and 37ưC
0.68
D-Glu

-
pH 8.3, 37ưC, recombinant DDO-3
0.8
D-Glu
-
pH 8.3, 37ưC, recombinant DDO-2
1.06
D-Glu
-
pH 8.3, 37ưC, recombinant DDO-1
2.6
D-Glu
pH 7.0, 20ưC, recombinant wild-type enzyme
6.77
D-Glu
-
pH 8.2, 37ưC, kidney
6.91
D-Glu
-
pH 8.2, 37ưC, brain
7.52
D-Glu
-
pH 8.2, 37ưC, liver
106
D-Glu
wild type enzyme, at pH 7.5 and 37ưC
106
D-Glu
pH 7.0, 20ưC, recombinant wild-type enzyme
0.23
D-glutamate

-
37ưC, pH 8.3, C47A10.5 gene product
0.23
D-glutamate
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37ưC
0.25
D-glutamate
-
37ưC, pH 8.3, F18E3.7a gene product
0.25
D-glutamate
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37ưC
0.59
D-glutamate
-
at pH 8.3
2.1
D-glutamate
-
at pH 7.4
5.7
D-glutamate
-
ferricyanide as acceptor
62.6
D-glutamate
37ưC, pH 7.5
166
D-glutamate
-
O2 as acceptor
600
D-glutamine

-
-
8.5
D-Met

mutant enzyme H56A, at pH 7.5 and 37ưC
31.8
D-Met
mutant enzyme H56N, at pH 7.5 and 37ưC
14.3
D-Phe

mutant enzyme H56A, at pH 7.5 and 37ưC
34.8
D-Phe
mutant enzyme H56N, at pH 7.5 and 37ưC
0.9
D-proline

-
-
2.85
N-methyl-D-Asp

-
pH 8.2, 37ưC, kidney
3.05
N-methyl-D-Asp
-
pH 8.2, 37ưC, brain
3.41
N-methyl-D-Asp
-
pH 8.2, 37ưC, liver
8.87
N-methyl-D-Asp
-
pH 8.3, 37ưC, recombinant DDO-3
9.23
N-methyl-D-Asp
-
pH 8.3, 37ưC, recombinant DDO-2
14.6
N-methyl-D-Asp
-
pH 8.3, 37ưC, recombinant DDO-1
15.7
N-methyl-D-Asp
pH 7.0, 20ưC, recombinant wild-type enzyme
27.9
N-methyl-D-Asp
pH 7.0, 20ưC, recombinant wild-type enzyme
0.84
N-methyl-D-asparagine

-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37ưC
1.84
N-methyl-D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37ưC
0.2
N-Methyl-D-aspartate

-
-
0.84
N-Methyl-D-aspartate
-
37ưC, pH 8.3, C47A10.5 gene product
1.5
N-Methyl-D-aspartate
-
-
1.84
N-Methyl-D-aspartate
-
37ưC, pH 8.3, F18E3.7a gene product
1.95
N-Methyl-D-aspartate
mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
2.67
N-Methyl-D-aspartate
His-tagged mutant enzyme S308G, at 37ưC 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 37ưC 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 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
6.8
N-Methyl-D-aspartate
-
-
7.81
N-Methyl-D-aspartate
mutant enzyme S308Y fused N-terminally with glutathione S-transferase, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
8.02
N-Methyl-D-aspartate
His-tagged wild type enzyme, at 37ưC in 40 mM sodium diphosphate buffer (pH 8.3)
28
N-Methyl-D-aspartate
-
-
42
N-Methyl-D-aspartate
-
-
47
N-Methyl-D-aspartate
-
-
47.7
N-Methyl-D-aspartate
-
-
85.3
N-Methyl-D-aspartate
37ưC, pH 7.5
0.17
O2

-
at 4ưC
0.547
O2
apparent value, using D-glutamate as substrate
0.613
O2
apparent value, using D-aspartate as substrate
2.01
O2
apparent value, using N-methyl-D-aspartate as substrate
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
-
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