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Information on EC 1.4.3.1 - D-aspartate oxidase and Organism(s) Caenorhabditis elegans and UniProt Accession Q19564
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1.4.3.1 D-aspartate oxidaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.4.3.1
-
d-amino
- n-methyl-d-aspartate
- nmda
- d-serine
- d-glutamate
- octopus
-
nmdar-dependent
- d-alanine
-
prepulse
- humicola
-
d-amino-acid
- d-ser
- d-glu
- drug development
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-aspartate oxidase, daspo, d-aspo, ddo-3, ddo-1, chddo, f18ep, c47ap, d-asp oxidase, chdaspo, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspartic oxidase
-
-
-
-
C47Ap
D-aspartic oxidase
-
-
-
-
DASOX
-
-
-
-
DASPO
F18Ep
C47Ap
-
the protein with DASPO activity shows distinct kinetic properties against D-Asp, D-Glu, and N-methyl-D-Asp
F18Ep
-
the protein with DASPO activity shows distinct kinetic properties against D-Asp, D-Glu, and N-methyl-D-Asp
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
D-aspartate:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9029-20-3
-
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
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
?
-
C47Ap exhibits 4.5% activity and F18Ep exhibits 2.8% activity compared to D-aspartate as substrate
-
-
?
D-arginine + H2O + O2
?
-
C47Ap exhibit less than 0.1% activity compared to D-aspartate as substrate
-
-
?
D-asparagine + H2O + O2
?
-
C47Ap exhibits 17% activity and F18Ep exhibits 6.1% activity compared to D-aspartate as substrate
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
preferred substrate
-
-
?
D-methionine + H2O + O2
?
-
C47Ap exhibits 3.8% activity and F18Ep exhibits 2.4% activity compared to D-aspartate as substrate
-
-
?
L-asparagine + H2O + O2
?
-
C47Ap exhibits 2.6% activity and F18Ep exhibits less than 0.1% activity compared to D-aspartate as substrate
-
-
?
L-glutamine + H2O + O2
?
-
C47Ap exhibits 1.3% activity and F18Ep exhibits 0.3% activity compared to D-aspartate as substrate
-
-
?
N-methyl-D-aspartate + 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
-
-
?
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-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
-
-
?
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
-
-
?
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
?
-
no substrates: D-Asn, D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Pro, D-Phe, D-Met, D-Trp, D-Cys, D-Lys, D-Arg, D-His, L-Asp, L-Glu, LAsn, 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-Cys, L-Lys, L-Arg, L-His, and Gly
-
-
-
additional information
?
-
-
no substrates: D-Asn, D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Pro, D-Phe, D-Met, D-Trp, D-Cys, D-Lys, D-Arg, D-His, L-Asp, L-Glu, LAsn, 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-Cys, L-Lys, L-Arg, L-His, and Gly
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-Glu + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
preferred 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
-
-
?
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
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
one molecule of FAD is noncovalently bound to one molecule of DDO
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics in comparison to the human DDO, overview
-
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
0.23
D-glutamate
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
0.25
D-glutamate
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
0.84
N-methyl-D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
1.84
N-methyl-D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.07
D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
4.29
D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
2.11
D-glutamate
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
5.31
D-glutamate
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
3
N-methyl-D-asparagine
-
recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
6.13
N-methyl-D-asparagine
-
recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
DDO3 is secreted from the cells where it is produced into the body fluid and taken up by scavenger coelomocytes
additional information
additional information
in males, DDO3 is secreted from the seminal vesicle into the seminal fluid in a signal peptide-dependent manner during mating with hermaphrodites. In hermaphrodites, DDO3 is secreted from the proximal gonadal sheath cells in a signal peptide-dependent manner and transferred to the oocyte surface
additional information
-
in males, DDO3 is secreted from the seminal vesicle into the seminal fluid in a signal peptide-dependent manner during mating with hermaphrodites. In hermaphrodites, DDO3 is secreted from the proximal gonadal sheath cells in a signal peptide-dependent manner and transferred to the oocyte surface
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
in hermaphrodites, DDO3 is secreted from the proximal gonadal sheath cells in a signal peptide-dependent manner and transferred to the oocyte surface. In males, DDO3 is secreted from the seminal vesicle into the seminal fluid in a signal peptide-dependent manner during mating with hermaphrodites. DDO3 is secreted from the cells where it is produced into the body fluid and taken up by scavenger coelomocytes
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
physiological function
-
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
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
the isoform responsible for in vivo metabolism of D-glutamate is DDO3, which is also required for normal self-fertility, hatching, and lifespan
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OXDD2_CAEEL
334
0
37608
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37607
-
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation
37636
-
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation
42501
-
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant DDO-1, DDO-2, and DDO-3 from Escherichia coli to homogeneity or near homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Katane, M.; Seida, Y.; Sekine, M.; Furuchi, T.; Homma, H.
Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases
FEBS J.
274
137-149
2007
Caenorhabditis elegans
Katane, M.; Saitoh, Y.; Seida, Y.; Sekine, M.; Furuchi, T.; Homma, H.
Comparative characterization of three D-aspartate oxidases and one D-amino acid oxidase from Caenorhabditis elegans
Chem. Biodivers.
7
1424-1434
2010
Caenorhabditis elegans
Katane, M.; Homma, H.
D-aspartate oxidase: The sole catabolic enzyme acting on free D-aspartate in mammals
Chem. Biodivers.
7
1435-1449
2010
Bos taurus, Caenorhabditis elegans, Vanrija humicola, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Saitoh, Y.; Katane, M.; Kawata, T.; Maeda, K.; Sekine, M.; Furuchi, T.; Kobuna, H.; Sakamoto, T.; Inoue, T.; Arai, H.; Nakagawa, Y.; Homma, H.
Spatiotemporal localization of D-amino acid oxidase and D-aspartate oxidases during development in Caenorhabditis elegans
Mol. Cell. Biol.
32
1967-1983
2012
Caenorhabditis elegans, Caenorhabditis elegans (O45307), Caenorhabditis elegans (Q19564), Caenorhabditis elegans N2, Caenorhabditis elegans N2 (O45307), Caenorhabditis elegans N2 (Q19564)
Katane, M.; Kuwabara, H.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.
Biochemical characterization of d-aspartate oxidase from Caenorhabditis elegans its potential use in the determination of free D-glutamate in biological samples
Biochim. Biophys. Acta
1868
140442
2020
Caenorhabditis elegans (O45307), Caenorhabditis elegans
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