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
Asterotremella humicola
strain UJ1
-
-
Manually annotated by BRENDA team
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
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-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-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-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-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-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-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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
-
10% activity when FAD is replaced with FMN
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
2-oxoglutaric acid
-
at 6.67 mM 64% inhibition
adipic acid
-
at 6.67 mM 15% inhibition
Benzoate
Citric acid
-
at 6.67 mM 29% inhibition
D-malate
D-Tartaric acid
-
at 6.67 mM 77% inhibition
Fumaric acid
-
at 6.67 mM 78% inhibition
Glutaric acid
-
at 6.67 mM 62% inhibition
KCN
-
-
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
meso-tartrate
N-Methyl-D-aspartate
substrate inhibition
oxalic acid
-
at 6.67 mM 40% inhibition
oxaloacetic acid
-
at 6.67 mM 90% inhibition
succinic acid
-
at 6.67 mM 66% inhibition
thiolactomycin
additional information
-
benzoate has no inhibitory effect
-
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
Asterotremella humicola
-
pH and temperature not specified in the publication
16.2
D-alpha-aminoadipic acid
-
-
1 - 13.4
D-Asp
0.38 - 240
D-asparagine
0.86 - 7.7
D-Aspartate
150 - 540
D-aspartate dimethylester
3
D-aspartic acid-beta-hydroxamate
-
-
0.68 - 106
D-Glu
0.23 - 166
D-glutamate
600 - 815
D-glutamine
9.8
D-homocysteic acid
-
-
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
Asterotremella humicola
-
pH and temperature not specified in the publication
1.3 - 121
D-Asp
3.07 - 4.29
D-asparagine
0.183 - 82.6
D-Aspartate
0.76 - 35.4
D-Glu
2 - 5.31
D-glutamate
1.52 - 84.5
N-methyl-D-Asp
3 - 6.13
N-methyl-D-asparagine
6.13 - 38.1
N-Methyl-D-aspartate
30 - 635
O2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
136 - 121000
D-Asp
1465
24 - 33440
D-Glu
1178
172 - 5787
N-methyl-D-Asp
6383
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, 37C
0.011 - 13.3
D-malate
0.06 - 5.4
malonate
1.94 - 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, 37C
5.3
malonate
Mus musculus
-
pH 8.3, 37C
8.71
meso-tartrate
Mus musculus
-
pH 8.3, 37C
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
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243E, substrate N-methyl-D-Asp; pH 7.0, 20C, purified recombinant mutant R243K, substrate N-methyl-D-Asp
0.08
unpurified recombinant enzyme
0.09
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243A, substrate D-Asp
0.1
wild type enzyme, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.11
mutant enzyme S308Y, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.24
mutant enzyme S308A, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
0.4
-
-
0.5
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243K, substrate D-Glu
0.55
mutant enzyme S308G, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate
1
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243E, substrate D-Glu
1.2
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243D, substrate N-methyl-D-Asp
1.5
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243K, substrate D-Asp
1.6
Asterotremella humicola
pH 7.0, 20C, purified recombinant wild-type enzyme, substrate D-Glu
1.9
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243E, substrate D-Asp
2.37
mutant enzyme S308Y, at 37C 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 37C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
4.31
wild type enzyme, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
4.32
wild type enzyme, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
5.55
mutant enzyme S308A, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
5.92
mutant enzyme S308A, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate
9.2
Asterotremella humicola
pH 7.0, 20C, purified recombinant wild-type enzyme, substrate N-methyl-D-Asp
9.24
mutant enzyme S308G, at 37C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate
18.5
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243D, substrate D-Glu
25.3
-
-
29.1
-
-
62
recombinant enzyme after 775fold purification
76.1
Asterotremella humicola
-
-
86
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243M, substrate D-Asp
93.7
Asterotremella humicola
pH 7.0, 20C, purified recombinant wild-type enzyme, substrate D-Asp
123
Asterotremella humicola
-
181
Asterotremella humicola
pH 7.0, 20C, purified recombinant mutant R243D, substrate D-Asp
additional information
Asterotremella humicola
mutant activities with D-Ala and D-Arg, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
Asterotremella humicola
assay at
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
6.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
Asterotremella humicola
assay at
33 - 37
Asterotremella humicola
-
-
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
-
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
-
in the cell bodies of the neurons
Manually annotated by BRENDA team
-
primary cultured
Manually annotated by BRENDA team
-
pheochromocytoma cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in magnocellular neurons of the rat supraoptic nucleus, but not in other subcellular structures of the nucleus and soma, including the nucleoplasm and cytoplasm
Manually annotated by BRENDA team
-
in magnocellular neurons of the rat supraoptic nucleus
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
native PAGE
37610
-
F18Ep, calculated from sequence of cDNA
37620
-
calculated from amino acid sequence
37640
-
C47Ap, calculated from sequence of cDNA
37660
-
apoprotein, amino acid analysis
38000
-
recombinant protein, SDS-PAGE
39000
-
containing 1 molecule of FAD, SDS-PAGE
40000
Asterotremella humicola
-
SDS-PAGE
41770
-
His-tagged F18Ep, calculated from sequence of cDNA
41790
-
His-tagged C47Ap, calculated from sequence of cDNA
146000
low-angle laser light scattering photometry
152000
SDS-PAGE
164000
Asterotremella humicola
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
tetramer
Asterotremella humicola
4 * 39459, deduced from nucleotide sequence; 4 * 40000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 510%(w/v) PEG 8000, 100 mM sodium dihydrogen phosphate (or 100 mM potassium dihydrogen phosphate), 100 mM sodium acetate (pH 4.7)
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
fairly stable
391727
7.5 - 9
the activity increases gradually as pH increases from pH 5.5 to 7.5, exhibits an almost constant value over pH 7.5 to 9.0, and decreases as the pH increases over pH 9.0
687440
9
-
stable
391715
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
Asterotremella humicola
little loss of activity
60
Asterotremella humicola
complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, deionized water, several days, 100% activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, mixture of 80-91% active FAD-containing and 9-20% inactive OH-FAD containing enzyme
-
His GraviTrap column chromatography
HiTrap Chelating HP column chromatography; recombinant C47A10.5 gene product; recombinant F18E3.7a gene product
-
recombinant
-
recombinant chDDO, ammonium sulfate, Butyl-Sepharose, SP-Sepharose
Asterotremella humicola
recombinant DDO-1, DDO-2, and DDO-3 from Escherichia coli to homogeneity or near homogeneity
-
recombinant enzyme
Asterotremella humicola
-
recombinant enzyme from Escherichia coli
recombinant His-tagged wild-type and mutant DDOs from Escherichia coli strain Rosetta (DE3) by metal affinity chromatography and gel filtration
Asterotremella humicola
SP-Toyopearl column chromatography, Q-Sepharose column chromatography, PPG-Toyopearl column chromatography, and SuperSW3000 gel filtration
TSK gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Asterotremella humicola
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21
-
expressed in Escherichia coli BL21 Star (DE 3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli GI724 cells
-
expressed in Escherichia coli strain BL21(DE3)pLysS
expressed in Escherichia coli strains BL21(DE3)pLysS and JM 109
-
expression in Escherichia coli
Asterotremella humicola
expression of GST-tagged, N-terminally His-tagged, and S-tagged DDO
-
expression of His-tagged wild-type and mutant DDOs in Escherichia coli strain Rosetta (DE3)
Asterotremella humicola
from brain, expressed in Escherichia coli
-
from kidney, expressed in Escherichia coli
genes F20Hp, C47Ap, and F18Ep, expression of DDO-1, DDO-2, and DDO-3 in Escherichia coli
-
the C47A10.5 gene product is expressed in Escherichia coli as recombinant protein with an N-terminal His-tag; the F18E3.7a gene product is expressed in Escherichia coli as recombinant protein with an N-terminal His-tag; the His-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chronic D-Asp treatment leads to upregulation of D-AspO expression in all tissues, along with up- or downregulation of superoxide dismutase 1 and caspase 3 depending on the tissues, overview. D-Asp treated kidney showed the highest D-AspO activity
-
D-Asp specifically triggers D-AspO activity
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R243A