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Information on EC 1.4.3.1 - D-aspartate oxidase and Organism(s) Sus scrofa and UniProt Accession A3KCL7
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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: Sus scrofa
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, d-asp oxidase, f18ep, c47ap, ddo-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspartic oxidase
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-
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D-aspartic oxidase
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-
-
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DASOX
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
D-aspartate:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9029-20-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding
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?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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in the first step of the reaction, which is the only enzymatic step of the whole reaction scheme, DDO catalyzes the dehydrogenation of a D-amino acid to generate the corresponding imino acid, coupled with the reduction of FAD. Subsequently, FAD reoxidizes spontaneously in the presence of O2, producing H2O2, while the imino acid nonenzymatically hydrolyzes to 2-oxo acid and NH3
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-
?
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
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Aspartate
substrate activation at D-aspartate concentrations above 0.2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
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
-
growth hormone-positive cells and almost all proopiomelanocortin-positive cells
additional information
additional information
-
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). OXDD_PIG
341
1
37316
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SP-Toyopearl column chromatography, Q-Sepharose column chromatography, PPG-Toyopearl column chromatography, and SuperSW3000 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jaroszewicz, L.
D-Asparatate oxidase in the thyroid gland
Enzyme
20
80-89
1975
Sus scrofa
Still, J.L.; Sperling, E.
On the prosthetic group of the D-aspartic oxidase
J. Biol. Chem.
182
585-589
1950
Oryctolagus cuniculus, Ovis aries, Sus scrofa
-
Yamamoto, A.; Tanaka, H.; Ishida, T.; Horiike, K.
Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation
J. Biochem.
141
363-376
2007
Sus scrofa (A3KCL7), Sus scrofa
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
Yamamoto, A.; Tanaka, H.; Ishida, T.; Horiike, K.
D-aspartate oxidase localisation in pituitary and pineal glands of the female pig
J. Neuroendocrinol.
22
1165-1172
2010
Sus scrofa
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