Information on EC 1.4.3.1 - D-aspartate oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.4.3.1
-
RECOMMENDED NAME
GeneOntology No.
D-aspartate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alanine metabolism
-
-
Alanine, aspartate and glutamate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
D-aspartate:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9029-20-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
anglerfish
-
-
Manually annotated by BRENDA team
saury
-
-
Manually annotated by BRENDA team
yellow sea bream
-
-
Manually annotated by BRENDA team
strain elongantum Y-105
-
-
Manually annotated by BRENDA team
japanese sea perch
-
-
Manually annotated by BRENDA team
kuruma prawn
-
-
Manually annotated by BRENDA team
hard clam
-
-
Manually annotated by BRENDA team
scallop
-
-
Manually annotated by BRENDA team
mussel
-
-
Manually annotated by BRENDA team
no activity in Rubrobacter xylanophilus
-
-
-
Manually annotated by BRENDA team
chum salmon
-
-
Manually annotated by BRENDA team
land-locked masu salmon
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
olive flounder
-
-
Manually annotated by BRENDA team
smelt fish
-
-
Manually annotated by BRENDA team
crayfish
-
-
Manually annotated by BRENDA team
marbled sole
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
sardine
-
-
Manually annotated by BRENDA team
chub mackerel
-
-
Manually annotated by BRENDA team
filefish
-
-
Manually annotated by BRENDA team
flying squid
-
-
Manually annotated by BRENDA team
horse mackerel
-
-
Manually annotated by BRENDA team
turban shell
-
-
Manually annotated by BRENDA team
right-eyed flounder
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
cis-2,3-piperidine dicarboxylic acid + H2O + O2
?
show the reaction diagram
-
-
-
-
?
cis-2,3-piperidinedicarboxylate + H2O + O2
?
show the reaction diagram
D-alanine + H2O + O2
?
show the reaction diagram
D-alpha-aminoadipic acid + H2O + O2
2-oxoadipic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
D-aminoadipate + H2O + O2
?
show the reaction diagram
D-arginine + H2O + O2
?
show the reaction diagram
-
C47Ap exhibit less than 0.1% activity compared to D-aspartate as substrate
-
-
?
D-Asn + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
show the reaction diagram
D-Asn + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
substrate for mutant enzyme H56N
-
-
?
D-Asn + H2O + O2
oxaloacetate + NH3 + H2O2
show the reaction diagram
-
low activity
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
show the reaction diagram
D-asparagine + H2O + O2
2-oxosuccinamic acid + H2O2 + NH3
show the reaction diagram
D-asparagine + H2O + O2
?
show the reaction diagram
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
show the reaction diagram
D-aspartate dimethylester + H2O + O2
oxaloacetic acid dimethylester + H2O2 + NH3
show the reaction diagram
D-aspartic acid-beta-hydroxamate + H2O + O2
4-(hydroxyamino)-2,4-dioxobutanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
D-Gln + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
substrate for mutant enzymes H56A and H56N
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + H2O2 + NH3
show the reaction diagram
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
show the reaction diagram
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
show the reaction diagram
D-glutamine + H2O + O2
2-oxoglutaric acid + H2O2 + NH3
show the reaction diagram
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram
D-homocysteic acid + H2O + O2
2-oxo-4-mercapto-butanoate
show the reaction diagram
D-homocysteic acid + H2O + O2
2-oxo-4-sulfobutanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
D-hydroxyglutarate + H2O + O2
?
show the reaction diagram
D-Leu + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
substrate for mutant enzyme H56N
-
-
?
D-Met + H2O + O2
4-(methylsulfonyl)-2-oxobutanoate + NH3 + H2O2
show the reaction diagram
-
substrate for mutant enzymes H56A and H56N
-
-
?
D-methionine + H2O + O2
4-(methylsulfonyl)-2-oxobutanoic acid + NH3 + H2O2
show the reaction diagram
-
1.8% activity compared to D-aspartate
-
-
?
D-methionine + H2O + O2
?
show the reaction diagram
-
C47Ap exhibits 3.8% activity and F18Ep exhibits 2.4% activity compared to D-aspartate as substrate
-
-
?
D-Phe + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
substrate for mutant enzymes H56A and H56N
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
D-thiazolidine-2-carboxylate + H2O + O2
(ethylthio)oxoacetic acid + H2O2 + NH3
show the reaction diagram
-
-
-
-
?
DL-2-amino-3-phosphonopropanoic acid + H2O + O2
2-oxo-3-phosphonopropanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
DL-cysteic acid + H2O + O2
2-oxo-3-sulfopropionic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
glycyl-D-aspartic acid + H2O + O2
?
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O + O2
?
show the reaction diagram
-
C47Ap exhibits 2.6% activity and F18Ep exhibits less than 0.1% activity compared to D-aspartate as substrate
-
-
?
L-glutamine + H2O + O2
?
show the reaction diagram
-
C47Ap exhibits 1.3% activity and F18Ep exhibits 0.3% activity compared to D-aspartate as substrate
-
-
?
meso-2,3-diaminosuccinate + H2O + O2
?
show the reaction diagram
N-acetyl-DL-aspartate + H2O + O2
oxaloacetate + acetylamine + H2O2
show the reaction diagram
N-methyl-D-Asp + H2O + O2
oxaloacetate + methylamine + H2O2
show the reaction diagram
N-methyl-D-aspartate + H2O + O2
oxaloacetate + CH3NH2 + H2O2
show the reaction diagram
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
show the reaction diagram
N-methyl-D-Glu + H2O + O2
2-oxoglutarate + methylamine + H2O2
show the reaction diagram
N-methyl-L-Asp + + H2O + O2
oxaloacetate + methylamine + H2O2
show the reaction diagram
N-methyl-L-asparagine + H2O + O2
?
show the reaction diagram
-
C47Ap exhibits 6.7% activity and F18Ep exhibits 1.1% activity compared to D-aspartate as substrate
-
-
?
N-methyl-L-aspartate + H2O + O2
?
show the reaction diagram
-
4% activity compared to D-aspartate
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
show the reaction diagram
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
show the reaction diagram
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
show the reaction diagram
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
show the reaction diagram
-
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
show the reaction diagram
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
show the reaction diagram
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
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
-
10% activity when FAD is replaced with FMN
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
not influenced by Na+, K+, Mg2+, Ca2+, Co2+, Mn2+, and Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
1-hydroxy-1H-indole-2-carboxylic acid
-
-
2-amino-5-chlorobenzoic acid
-
-
2-amino-5-methylthiophene-3-carboxylic acid
-
-
-
2-aminopyridine-3-carboxylic acid
-
-
2-aminopyridine-4-carboxylic acid
-
-
2-hydroxy-6-methylpyridine-3-carboxylic acid
-
-
2-oxoglutaric acid
-
at 6.67 mM 64% inhibition
3-aminobenzoic acid
-
-
3-aminopyridine-2-carboxylic acid
-
-
3-aminopyridine-4-carboxylic acid
-
-
3-hydroxypyridine-2-carboxylic acid
-
-
4-aminopyridine-2-carboxylic acid
-
-
4-aminopyridine-3-carboxylic acid
-
-
4-carbamoylthiophene-2-carboxylic acid
-
-
5-(dimethylamino)pyridine-3-carboxylic acid
-
-
5-(methylamino)pyridine-3-carboxylic acid
-
-
5-(trifluoromethyl)pyridine-3-carboxylic acid
-
-
5-aminonicotinic acid
-
-
-
5-aminopyridine-2-carboxylic acid
-
-
5-bromopyridine-3-carboxylic acid
-
-
5-chloro-2-hydroxybenzoic acid
-
-
5-chloropyridine-3-carboxylic acid
-
-
5-fluoro-2-hydroxybenzoic acid
-
-
5-fluoropyridine-3-carboxylic acid
-
-
5-hydroxypyridine-3-carboxylic acid
-
-
5-methoxypyridine-3-carboxylic acid
-
-
5-methylpyridine-3-carboxylic acid
-
-
5-nitropyridine-3-carboxylic acid
-
-
5-phenylpyridine-3-carboxylic acid
-
-
5-sulfopyridine-3-carboxylic acid
-
-
6-aminopyridine-2-carboxylic acid
-
-
6-aminopyridine-3-carboxylic acid
-
-
7-hydroxy-4-hydro-1,2,4-triazolo[4,3-a]pyrimidine-6-carboxylic acid
-
-
-
adipic acid
-
at 6.67 mM 15% inhibition
Aminooxyacetate
Benzoate
Benzoic acid
-
-
Citric acid
-
at 6.67 mM 29% inhibition
Cu2+
-
90.7% residual activity at 1 mM
D-malate
D-Tartaric acid
-
at 6.67 mM 77% inhibition
Fe2+
-
86.5% residual activity at 1 mM
Fumaric acid
-
at 6.67 mM 78% inhibition
Glutaric acid
-
at 6.67 mM 62% inhibition
KCN
-
-
L-Glu
-
89.3% residual activity at 1 mM
L-leucine
-
6% inhibition at 6.67 mM
L-Malic acid
-
at 6.67 mM 79% inhibition
L-Tartaric acid
-
at 6.67 mM 24% inhibition
L-Tartrate
L-valine
-
6% inhibition at 6.67 mM
malate
-
52% inhibition at 50 mM
malonate
malonic acid
-
-
meso-tartrate
N-Methyl-D-aspartate
substrate inhibition
Ni2+
-
93.3% residual activity at 1 mM
olanzapine
oxalic acid
-
at 6.67 mM 40% inhibition
oxaloacetic acid
-
at 6.67 mM 90% inhibition
pyridin-3-amine
-
-
pyridine-3,5-dicarboxylic acid
-
-
pyridine-3-carboxylic acid
-
-
pyridoxal 5'-phosphate
-
93.5% residual activity at 0.2 mM
succinic acid
-
at 6.67 mM 66% inhibition
thiolactomycin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-Aspartate
substrate activation at D-aspartate concentrations above 0.2 mM
D-Glu
substrate activation at D-glutamate concentrations above 4 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 37°C
1 - 13.4
D-Asp
0.38 - 240
D-asparagine
0.38 - 7.7
D-Aspartate
150 - 540
D-aspartate dimethylester
3
D-aspartic acid-beta-hydroxamate
-
-
21 - 39.4
D-Gln
0.68 - 106
D-Glu
0.23 - 166
D-glutamate
600 - 815
D-glutamine
9.8
D-homocysteic acid
-
-
8.8
D-Leu
-
mutant enzyme H56N, at pH 7.5 and 37°C
8.5 - 31.8
D-Met
14.3 - 34.8
D-Phe
0.9 - 440
D-proline
15.2
DL-amino-3-phosphopropanoic acid
-
-
1.7
DL-cysteic 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
0.17 - 2.01
O2
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.62
D-alanine
-
pH and temperature not specified in the publication
3.9
D-Asn
-
mutant enzyme H56N, at pH 7.5 and 37°C
1.3 - 121
D-Asp
3.07 - 4.29
D-asparagine
0.183 - 82.6
D-Aspartate
2.2 - 4.5
D-Gln
0.76 - 35.4
D-Glu
2 - 5.31
D-glutamate
0.7
D-Leu
-
mutant enzyme H56N, at pH 7.5 and 37°C
4 - 11.5
D-Met
3.1 - 4.1
D-Phe
1.52 - 84.5
N-methyl-D-Asp
3 - 6.13
N-methyl-D-asparagine
3 - 38.1
N-Methyl-D-aspartate
30 - 635
O2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047
D-Asn
-
mutant enzyme H56N, at pH 7.5 and 37°C
1.354 - 121000
D-Asp
0.055 - 0.213
D-Gln
0.024 - 33440
D-Glu
0.074
D-Leu
-
mutant enzyme H56N, at pH 7.5 and 37°C
0.125 - 1.35
D-Met
0.119 - 0.218
D-Phe
172 - 5787
N-methyl-D-Asp
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0038
5-aminonicotinic acid
-
at pH 8.3 and 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
-
1.416 - 1.915
Aminooxyacetate
0.011 - 13.3
D-malate
0.06 - 5.4
malonate
0.153
malonic acid
-
at pH 8.3 and 37°C
0.472 - 61
meso-tartrate
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
10
2-amino-5-chlorobenzoic acid
Homo sapiens
-
IC50 above 10 mM, at pH 8.3 and 37°C
1
2-aminopyridine-3-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-aminobenzoic acid
Homo sapiens
-
IC50 above 10 mM, at pH 8.3 and 37°C
1
3-aminopyridine-2-carboxylic acid
Homo sapiens
-
IC50 above 1 mM, at pH 8.3 and 37°C
5
3-aminopyridine-4-carboxylic acid
Homo sapiens
-
IC50 above 5 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
3.541
5-(methylamino)pyridine-3-carboxylic acid
Homo sapiens
-
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
0.0219
5-aminonicotinic acid
Homo sapiens
-
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-chloro-2-hydroxybenzoic 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-fluoro-2-hydroxybenzoic 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
3.351
5-hydroxypyridine-3-carboxylic acid
Homo sapiens
-
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
5.472
5-methylpyridine-3-carboxylic acid
Homo sapiens
-
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
2.364
6-aminopyridine-3-carboxylic acid
Homo sapiens
-
at pH 8.3 and 37°C
5.3
malonate
Mus musculus
-
pH 8.3, 37°C
8.71
meso-tartrate
Mus musculus
-
pH 8.3, 37°C
0.0014 - 0.0231
olanzapine
10
pyridin-3-amine
Homo sapiens
-
IC50 above 10 mM, at pH 8.3 and 37°C
10
pyridine-3,5-dicarboxylic acid
Homo sapiens
-
IC50 above 10 mM, at pH 8.3 and 37°C
2.778
pyridine-3-carboxylic acid
Homo sapiens
-
at pH 8.3 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00021
-
from kidney
0.00048
-
from liver
0.00053
-
from brain
0.00055
-
from liver
0.0006
-
from kidney
0.00062
-
from kidney
0.00076
-
from kidney
0.00119
0.00144
-
from liver
0.00233
-
from liver
0.0035
-
-
0.04
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
0.08
unpurified recombinant enzyme
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
0.12
-
with D-Pro as substrate, at pH 8.3 and 37°C
0.14
-
with D-His as substrate, at pH 8.3 and 37°C
0.16
-
with D-Asn as substrate, at pH 8.3 and 37°C
0.24
-
mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.4
-
-
0.46
-
with D-Glu as substrate, at pH 8.3 and 37°C
0.47
-
with N-methyl-L-Asp as substrate, at pH 8.3 and 37°C
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
pH 7.0, 20°C, purified recombinant mutant R243E, substrate D-Glu
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
2.37
-
mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
2.4
-
ferricyanide as electron acceptor
2.54
-
mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
2.93
-
with D-Asn as substrate, at pH 8.3 and 37°C
3.17
-
with N-methyl-D-Glu as substrate, at pH 8.3 and 37°C
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
7.82
-
with D-Glu as substrate, at pH 8.3 and 37°C
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
12.2
-
with D-Asp as substrate, at pH 8.3 and 37°C
18.5
pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Glu
25.3
-
-
29.1
-
-
62
recombinant enzyme after 775fold purification
86
pH 7.0, 20°C, purified recombinant mutant R243M, substrate D-Asp
87.5
-
with D-Asp as substrate, at pH 8.3 and 37°C
91.2
-
with N-methyl-D-Asp as substrate, at pH 8.3 and 37°C
93.7
pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Asp
181
pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Asp
additional information
mutant activities with D-Ala and D-Arg, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
-
-
additional information
-
optimum depends on the order of addition of the reactands
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11
-
largely destroyed below or over this range
5 - 9
-
activity assay range
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
6.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33 - 37
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
relatively high enzyme expression just after birth, the content gradually decreases thereafter
Manually annotated by BRENDA team
-
504 hours old
Manually annotated by BRENDA team
-
primary cultured
Manually annotated by BRENDA team
-
pheochromocytoma cells
Manually annotated by BRENDA team
additional information