BRENDA - Enzyme Database
show all sequences of 1.4.3.1

D-aspartate oxidase: The sole catabolic enzyme acting on free D-aspartate in mammals

Katane, M.; Homma, H.; Chem. Biodivers. 7, 1435-1449 (2010)

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
a DDO inhibitor that augments brain D-Asp levels can be a potent antipsychotic drug for the treatment of NMDA receptor-related disease
Homo sapiens
drug development
a DDO inhibitor that augments brain D-Asp levels can be a potent antipsychotic drug for the treatment of NMDA receptor-related disease
Mus musculus
Cloned(Commentary)
Commentary
Organism
-
Vanrija humicola
from brain, expressed in Escherichia coli
Homo sapiens
from kidney, expressed in Escherichia coli
Bos taurus
from kidney, expressed in Escherichia coli
Mus musculus
from kidney, expressed in Escherichia coli
Sus scrofa
Engineering
Amino acid exchange
Commentary
Organism
additional information
intense D-Asp immunoreactivity is observed in the intermediate lobe of the pituitary gland of the DDO-deficient mice, phenotype of DDO-deficient mice, detailed overview
Mus musculus
R216X
activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg216 residue with other amino acid residues
Mus musculus
R237X
activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg237 residue with other amino acid residues
Mus musculus
S308G
the mutation results in lack of a side-chain OH group at position 308, and increases mutant enzyme catalytic efficiency against D-Asp and NMDA to about 7-10times higher than that of the wild-type enzyme. Moreover, the dissociation-constant value for FAD of this Gly-substitution mutant is significantly lower than that of the wild-type enzyme, suggesting that it has enhanced ability to bind to FAD
Mus musculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
malonate
-
Bos taurus
malonate
-
Caenorhabditis elegans
malonate
-
Ovis aries
malonate
-
Sus scrofa
malonate
-
Vanrija humicola
malonate
-
Homo sapiens
malonate
-
Mus musculus
malonate
-
Rattus norvegicus
meso-tartrate
-
Bos taurus
meso-tartrate
-
Caenorhabditis elegans
meso-tartrate
-
Ovis aries
meso-tartrate
-
Sus scrofa
meso-tartrate
-
Vanrija humicola
meso-tartrate
-
Homo sapiens
meso-tartrate
-
Mus musculus
meso-tartrate
-
Rattus norvegicus
thiolactomycin
-
Bos taurus
thiolactomycin
-
Caenorhabditis elegans
thiolactomycin
-
Homo sapiens
thiolactomycin
-
Mus musculus
thiolactomycin
-
Ovis aries
thiolactomycin
-
Rattus norvegicus
thiolactomycin
-
Sus scrofa
thiolactomycin
-
Vanrija humicola
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
axon
-
Rattus norvegicus
30424
-
cytoplasm
DDO-2
Caenorhabditis elegans
5737
-
extracellular
DDO-3
Caenorhabditis elegans
-
-
heterochromatin
in magnocellular neurons of the rat supraoptic nucleus, but not in other subcellular structures of the nucleus and soma, including the nucleoplasm and cytoplasm
Rattus norvegicus
792
-
nucleolus
in magnocellular neurons of the rat supraoptic nucleus
Rattus norvegicus
5730
-
peroxisome
-
Bos taurus
5777
-
peroxisome
DDO-1
Caenorhabditis elegans
5777
-
peroxisome
-
Homo sapiens
5777
-
peroxisome
-
Mus musculus
5777
-
peroxisome
-
Ovis aries
5777
-
peroxisome
-
Rattus norvegicus
5777
-
peroxisome
-
Sus scrofa
5777
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-aspartate + H2O + O2
Mus musculus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Homo sapiens
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Rattus norvegicus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Sus scrofa
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Bos taurus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Ovis aries
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Caenorhabditis elegans
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Vanrija humicola
-
oxaloacetate + NH3 + H2O2
-
-
?
D-glutamate + H2O + O2
Caenorhabditis elegans
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
2-oxoglutarate + NH3 + H2O2
-
-
?
additional information
Caenorhabditis elegans
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
?
-
-
-
N-methyl-D-aspartate + H2O + O2
Mus musculus
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Homo sapiens
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Rattus norvegicus
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Sus scrofa
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Bos taurus
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Ovis aries
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Caenorhabditis elegans
-
oxaloacetate + methylamine + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Caenorhabditis elegans
-
at least three genes encoding functional DDO isozymes DDO-1, DDO-2, and DDO-3
-
Homo sapiens
-
-
-
Mus musculus
-
-
-
Ovis aries
-
-
-
Rattus norvegicus
-
-
-
Sus scrofa
-
-
-
Vanrija humicola
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme
Vanrija humicola
recombinant enzyme from Escherichia coli
Bos taurus
recombinant enzyme from Escherichia coli
Homo sapiens
recombinant enzyme from Escherichia coli
Mus musculus
recombinant enzyme from Escherichia coli
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
adrenal gland
adrenal cortex and adrenal medulla epinephrine cells
Mus musculus
-
adrenal gland
-
Rattus norvegicus
-
brain
cerebellar cortex Bergmann glia
Mus musculus
-
brain
embryonic, D-Asp initially emerges in the hindbrain and then spreads into the forebrain. Within nerve cells of the rat embryonic brain, D-Asp first occurs in the cell bodies of neuroblasts in the outer layer of the neuronal epithelium, and then it appears in the processes of the cells
Rattus norvegicus
-
cerebral cortex
relatively high enzyme expression just after birth, the content gradually decreases thereafter
Homo sapiens
-
cerebrum
relatively high enzyme expression just after birth, the content gradually decreases thereafter
Rattus norvegicus
-
follicular fluid
-
Homo sapiens
-
gastric juice
-
Homo sapiens
-
hippocampus
-
Mus musculus
-
hypothalamus
in the cell bodies of the neurons
Rattus norvegicus
-
kidney
-
Bos taurus
-
kidney
in Bowman's capsule, renal thin limbs of Henle's loop
Mus musculus
-
kidney
-
Ovis aries
-
kidney
-
Rattus norvegicus
-
kidney
-
Sus scrofa
-
Leydig cell
-
Mus musculus
-
liver
-
Homo sapiens
-
liver
-
Mus musculus
-
liver
-
Rattus norvegicus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Bos taurus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Homo sapiens
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Mus musculus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Ovis aries
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Rattus norvegicus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Sus scrofa
-
neuron
primary cultured
Rattus norvegicus
-
pancreas
-
Rattus norvegicus
-
PC-12 cell
pheochromocytoma cells
Rattus norvegicus
-
pineal gland
D-Asp content in the adult rat pineal gland is very high, especially in the distal (caudal) region of the gland, little staining is found in the proximal (rostral) region
Rattus norvegicus
-
pinealocyte
-
Rattus norvegicus
-
pituitary gland
intermediate lobe
Mus musculus
-
pituitary gland
prolactin-producing cells in the anterior lobe and microglial cells in the posterior lobe, D-Asp immunoreactivity is observed specifically in prolactin-producing mammotrophs or in a closely related cell type
Rattus norvegicus
-
retina
-
Mus musculus
-
retina
-
Rattus norvegicus
-
salivary gland
-
Homo sapiens
-
salivary gland
-
Rattus norvegicus
-
spermatozoon
-
Homo sapiens
-
testis
-
Mus musculus
-
testis
-
Rattus norvegicus
-
testis
-
Sus scrofa
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-aspartate + H2O + O2
-
711719
Mus musculus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Homo sapiens
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Rattus norvegicus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Sus scrofa
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Bos taurus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Ovis aries
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Caenorhabditis elegans
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Vanrija humicola
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Mus musculus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Homo sapiens
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Rattus norvegicus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Sus scrofa
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Bos taurus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Ovis aries
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Caenorhabditis elegans
oxaloacetate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
preferred substrate
711719
Caenorhabditis elegans
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
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
711719
Caenorhabditis elegans
2-oxoglutarate + NH3 + 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
711719
Caenorhabditis elegans
?
-
-
-
-
additional information
Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding
711719
Sus scrofa
?
-
-
-
-
additional information
Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding, overview
711719
Mus musculus
?
-
-
-
-
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
711719
Caenorhabditis elegans
?
-
-
-
-
N-methyl-D-aspartate + H2O + O2
-
711719
Mus musculus
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Homo sapiens
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Rattus norvegicus
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Sus scrofa
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Bos taurus
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Ovis aries
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Caenorhabditis elegans
oxaloacetate + methylamine + H2O2
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 37000-38000
Homo sapiens
?
x * 37000-38000
Mus musculus
?
x * 37000-38000
Rattus norvegicus
homotetramer
4 * 37000-38000
Sus scrofa
homotetramer
4 * 37000-38000
Vanrija humicola
monomer
1 * 37000-38000
Bos taurus
More
three-dimensional structure by homology-modeling
Mus musculus
More
three-dimensional structure by homology-modeling
Sus scrofa
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
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
Bos taurus
FAD
one molecule of FAD is noncovalently bound to one molecule of DDO
Caenorhabditis elegans
FAD
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
Homo sapiens
FAD
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
Mus musculus
FAD
one molecule of FAD is noncovalently bound to one molecule of DDO
Ovis aries
FAD
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
Rattus norvegicus
FAD
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
Sus scrofa
FAD
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
Vanrija humicola
Application (protein specific)
Application
Commentary
Organism
drug development
a DDO inhibitor that augments brain D-Asp levels can be a potent antipsychotic drug for the treatment of NMDA receptor-related disease
Homo sapiens
drug development
a DDO inhibitor that augments brain D-Asp levels can be a potent antipsychotic drug for the treatment of NMDA receptor-related disease
Mus musculus
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Vanrija humicola
from brain, expressed in Escherichia coli
Homo sapiens
from kidney, expressed in Escherichia coli
Bos taurus
from kidney, expressed in Escherichia coli
Mus musculus
from kidney, expressed in Escherichia coli
Sus scrofa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
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
Bos taurus
FAD
one molecule of FAD is noncovalently bound to one molecule of DDO
Caenorhabditis elegans
FAD
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
Homo sapiens
FAD
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
Mus musculus
FAD
one molecule of FAD is noncovalently bound to one molecule of DDO
Ovis aries
FAD
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
Rattus norvegicus
FAD
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
Sus scrofa
FAD
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
Vanrija humicola
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
intense D-Asp immunoreactivity is observed in the intermediate lobe of the pituitary gland of the DDO-deficient mice, phenotype of DDO-deficient mice, detailed overview
Mus musculus
R216X
activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg216 residue with other amino acid residues
Mus musculus
R237X
activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg237 residue with other amino acid residues
Mus musculus
S308G
the mutation results in lack of a side-chain OH group at position 308, and increases mutant enzyme catalytic efficiency against D-Asp and NMDA to about 7-10times higher than that of the wild-type enzyme. Moreover, the dissociation-constant value for FAD of this Gly-substitution mutant is significantly lower than that of the wild-type enzyme, suggesting that it has enhanced ability to bind to FAD
Mus musculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
malonate
-
Bos taurus
malonate
-
Caenorhabditis elegans
malonate
-
Homo sapiens
malonate
-
Mus musculus
malonate
-
Ovis aries
malonate
-
Rattus norvegicus
malonate
-
Sus scrofa
malonate
-
Vanrija humicola
meso-tartrate
-
Bos taurus
meso-tartrate
-
Caenorhabditis elegans
meso-tartrate
-
Homo sapiens
meso-tartrate
-
Mus musculus
meso-tartrate
-
Ovis aries
meso-tartrate
-
Rattus norvegicus
meso-tartrate
-
Sus scrofa
meso-tartrate
-
Vanrija humicola
thiolactomycin
-
Bos taurus
thiolactomycin
-
Caenorhabditis elegans
thiolactomycin
-
Homo sapiens
thiolactomycin
-
Mus musculus
thiolactomycin
-
Ovis aries
thiolactomycin
-
Rattus norvegicus
thiolactomycin
-
Sus scrofa
thiolactomycin
-
Vanrija humicola
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
axon
-
Rattus norvegicus
30424
-
cytoplasm
DDO-2
Caenorhabditis elegans
5737
-
extracellular
DDO-3
Caenorhabditis elegans
-
-
heterochromatin
in magnocellular neurons of the rat supraoptic nucleus, but not in other subcellular structures of the nucleus and soma, including the nucleoplasm and cytoplasm
Rattus norvegicus
792
-
nucleolus
in magnocellular neurons of the rat supraoptic nucleus
Rattus norvegicus
5730
-
peroxisome
-
Bos taurus
5777
-
peroxisome
DDO-1
Caenorhabditis elegans
5777
-
peroxisome
-
Homo sapiens
5777
-
peroxisome
-
Mus musculus
5777
-
peroxisome
-
Ovis aries
5777
-
peroxisome
-
Rattus norvegicus
5777
-
peroxisome
-
Sus scrofa
5777
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-aspartate + H2O + O2
Mus musculus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Homo sapiens
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Rattus norvegicus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Sus scrofa
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Bos taurus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Ovis aries
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Caenorhabditis elegans
-
oxaloacetate + NH3 + H2O2
-
-
?
D-aspartate + H2O + O2
Vanrija humicola
-
oxaloacetate + NH3 + H2O2
-
-
?
D-glutamate + H2O + O2
Caenorhabditis elegans
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
2-oxoglutarate + NH3 + H2O2
-
-
?
additional information
Caenorhabditis elegans
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
?
-
-
-
N-methyl-D-aspartate + H2O + O2
Mus musculus
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Homo sapiens
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Rattus norvegicus
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Sus scrofa
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Bos taurus
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Ovis aries
-
oxaloacetate + methylamine + H2O2
-
-
?
N-methyl-D-aspartate + H2O + O2
Caenorhabditis elegans
-
oxaloacetate + methylamine + H2O2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Vanrija humicola
recombinant enzyme from Escherichia coli
Bos taurus
recombinant enzyme from Escherichia coli
Homo sapiens
recombinant enzyme from Escherichia coli
Mus musculus
recombinant enzyme from Escherichia coli
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
adrenal gland
adrenal cortex and adrenal medulla epinephrine cells
Mus musculus
-
adrenal gland
-
Rattus norvegicus
-
brain
cerebellar cortex Bergmann glia
Mus musculus
-
brain
embryonic, D-Asp initially emerges in the hindbrain and then spreads into the forebrain. Within nerve cells of the rat embryonic brain, D-Asp first occurs in the cell bodies of neuroblasts in the outer layer of the neuronal epithelium, and then it appears in the processes of the cells
Rattus norvegicus
-
cerebral cortex
relatively high enzyme expression just after birth, the content gradually decreases thereafter
Homo sapiens
-
cerebrum
relatively high enzyme expression just after birth, the content gradually decreases thereafter
Rattus norvegicus
-
follicular fluid
-
Homo sapiens
-
gastric juice
-
Homo sapiens
-
hippocampus
-
Mus musculus
-
hypothalamus
in the cell bodies of the neurons
Rattus norvegicus
-
kidney
-
Bos taurus
-
kidney
in Bowman's capsule, renal thin limbs of Henle's loop
Mus musculus
-
kidney
-
Ovis aries
-
kidney
-
Rattus norvegicus
-
kidney
-
Sus scrofa
-
Leydig cell
-
Mus musculus
-
liver
-
Homo sapiens
-
liver
-
Mus musculus
-
liver
-
Rattus norvegicus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Bos taurus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Homo sapiens
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Mus musculus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Ovis aries
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Rattus norvegicus
-
additional information
development-related patterns of D-Asp expression differ among various mammalian tissues, overview
Sus scrofa
-
neuron
primary cultured
Rattus norvegicus
-
pancreas
-
Rattus norvegicus
-
PC-12 cell
pheochromocytoma cells
Rattus norvegicus
-
pineal gland
D-Asp content in the adult rat pineal gland is very high, especially in the distal (caudal) region of the gland, little staining is found in the proximal (rostral) region
Rattus norvegicus
-
pinealocyte
-
Rattus norvegicus
-
pituitary gland
intermediate lobe
Mus musculus
-
pituitary gland
prolactin-producing cells in the anterior lobe and microglial cells in the posterior lobe, D-Asp immunoreactivity is observed specifically in prolactin-producing mammotrophs or in a closely related cell type
Rattus norvegicus
-
retina
-
Mus musculus
-
retina
-
Rattus norvegicus
-
salivary gland
-
Homo sapiens
-
salivary gland
-
Rattus norvegicus
-
spermatozoon
-
Homo sapiens
-
testis
-
Mus musculus
-
testis
-
Rattus norvegicus
-
testis
-
Sus scrofa
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-aspartate + H2O + O2
-
711719
Mus musculus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Homo sapiens
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Rattus norvegicus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Sus scrofa
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Bos taurus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Ovis aries
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Caenorhabditis elegans
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
-
711719
Vanrija humicola
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Mus musculus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Homo sapiens
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Rattus norvegicus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Sus scrofa
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Bos taurus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Ovis aries
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
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
711719
Caenorhabditis elegans
oxaloacetate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
preferred substrate
711719
Caenorhabditis elegans
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
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
711719
Caenorhabditis elegans
2-oxoglutarate + NH3 + 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
711719
Caenorhabditis elegans
?
-
-
-
-
additional information
Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding
711719
Sus scrofa
?
-
-
-
-
additional information
Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding, overview
711719
Mus musculus
?
-
-
-
-
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
711719
Caenorhabditis elegans
?
-
-
-
-
N-methyl-D-aspartate + H2O + O2
-
711719
Mus musculus
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Homo sapiens
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Rattus norvegicus
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Sus scrofa
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Bos taurus
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Ovis aries
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-D-aspartate + H2O + O2
-
711719
Caenorhabditis elegans
oxaloacetate + methylamine + H2O2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 37000-38000
Homo sapiens
?
x * 37000-38000
Mus musculus
?
x * 37000-38000
Rattus norvegicus
homotetramer
4 * 37000-38000
Sus scrofa
homotetramer
4 * 37000-38000
Vanrija humicola
monomer
1 * 37000-38000
Bos taurus
More
three-dimensional structure by homology-modeling
Mus musculus
More
three-dimensional structure by homology-modeling
Sus scrofa
General Information
General Information
Commentary
Organism
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
Rattus norvegicus
physiological function
relevance of D-Asp and DDO to NMDA receptor-related disease, D-Asp protects against sensorimotor-gating deficits, which are observed in schizophrenic patients, overview. D-Asp is important in the development and neurogenesis of the brain
Homo sapiens
physiological function
relevance of D-Asp and DDO to NMDA receptor-related disease, overview. Phenotype of DDO-deficient mice, DDO-deficient mice display significant deficits in prepulse inhibition, and exhibit reduced immobility time in the Porsolt forced-swim test, a model of depression, suggesting that the genetic ablation of DDO has a specific antidepressant action, overview
Mus musculus
physiological function
D-Asp is important in the development and neurogenesis of the brain. D-Asp plays a regulatory role in the synthesis and secretion of prolactin in the anterior lobe of the pituitary gland. D-Asp directly interacts with DNA and/or acts on nuclear protein(s) involved in the regulation of gene transcription, through which d-Asp controls gene expression in the hypothalamo-neurohypophyseal system
Rattus norvegicus
General Information (protein specific)
General Information
Commentary
Organism
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
Rattus norvegicus
physiological function
relevance of D-Asp and DDO to NMDA receptor-related disease, D-Asp protects against sensorimotor-gating deficits, which are observed in schizophrenic patients, overview. D-Asp is important in the development and neurogenesis of the brain
Homo sapiens
physiological function
relevance of D-Asp and DDO to NMDA receptor-related disease, overview. Phenotype of DDO-deficient mice, DDO-deficient mice display significant deficits in prepulse inhibition, and exhibit reduced immobility time in the Porsolt forced-swim test, a model of depression, suggesting that the genetic ablation of DDO has a specific antidepressant action, overview
Mus musculus
physiological function
D-Asp is important in the development and neurogenesis of the brain. D-Asp plays a regulatory role in the synthesis and secretion of prolactin in the anterior lobe of the pituitary gland. D-Asp directly interacts with DNA and/or acts on nuclear protein(s) involved in the regulation of gene transcription, through which d-Asp controls gene expression in the hypothalamo-neurohypophyseal system
Rattus norvegicus
Other publictions for EC 1.4.3.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742426
Florio
Tracking the evolution of epi ...
Mus musculus
Epigenetics
12
41-54
2017
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
743836
Sacchi
Olanzapine, but not clozapine ...
Homo sapiens, Mus musculus
Sci. Rep.
7
46288
2017
-
-
-
-
-
-
4
-
-
-
-
2
-
6
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
4
-
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
742805
Takahashi
Possible role of a histidine ...
Vanrija humicola
J. Biochem.
159
371-378
2016
-
-
1
-
5
-
3
10
-
-
-
1
-
3
-
-
-
-
-
-
-
-
9
1
-
-
-
10
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
3
-
10
-
-
-
1
-
-
-
-
-
-
-
-
9
1
-
-
-
10
-
-
-
-
-
-
-
-
10
10
743133
Punzo
Age-related changes in D-aspa ...
Mus musculus
J. Neurosci.
36
3064-3078
2016
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
742035
Katane
Characterization of the enzym ...
Homo sapiens, Mus musculus, Rattus norvegicus
Biol. Pharm. Bull.
38
298-305
2015
-
-
3
-
-
-
15
3
-
1
-
3
-
9
-
-
3
-
-
1
12
-
19
-
1
-
1
3
-
1
1
3
9
-
-
-
-
3
3
-
-
-
-
15
9
3
-
1
-
3
-
-
-
3
-
1
12
-
19
-
1
-
1
3
-
1
1
-
-
-
-
-
3
3
743063
Katane
Identification of novel D-asp ...
Homo sapiens
J. Med. Chem.
58
7328-7340
2015
-
-
1
-
-
-
37
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
33
-
-
1
-
-
-
-
33
37
3
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
743140
Han
Changes in D-aspartic acid an ...
Mus musculus
J. Pharm. Biomed. Anal.
116
47-52
2015
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
7
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
7
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
743350
Cristino
D-aspartate oxidase influence ...
Mus musculus
Neurobiol. Aging
36
1890-1902
2015
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
741688
Takahashi
A highly stable d-amino acid ...
no activity in Rubrobacter xylanophilus
Appl. Environ. Microbiol.
80
7219-7229
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
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723870
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1
1
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1
1
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724597
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Enzymatic assay for D-aspartic ...
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2
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725959
Saitoh
Spatiotemporal localization of ...
Caenorhabditis elegans, Caenorhabditis elegans N2
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1
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3
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6
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14
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6
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1
3
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711325
Katane
Thiolactomycin inhibits D-aspa ...
Homo sapiens, Mus musculus
Biochimie
92
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2010
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1
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1
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6
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2
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6
4
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4
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1
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1
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711718
Katane
Comparative characterization o ...
Caenorhabditis elegans
Chem. Biodivers.
7
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2010
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1
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10
3
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3
3
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4
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1
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1
1
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9
1
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1
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1
1
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10
3
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3
3
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1
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4
1
1
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9
1
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1
1
-
9
9
711719
Katane
D-aspartate oxidase: The sole ...
Bos taurus, Caenorhabditis elegans, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa, Vanrija humicola
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5
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24
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40
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28
8
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8
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2
5
8
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4
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24
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17
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5
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40
-
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28
8
-
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-
4
4
-
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711721
Burrone
Effects of D-aspartate treatme ...
Pelophylax esculentus
Chem. Biodivers.
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2010
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-
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5
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1
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1
2
2
1
-
-
711722
Topo
Thyroid hormones and D-asparti ...
Mus musculus, Rattus norvegicus
Chem. Biodivers.
7
1467-1478
2010
-
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2
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4
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2
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2
2
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di Giovanni
Distribution of free D-asparti ...
Pelophylax esculentus
J. Exp. Zool.
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137-143
2010
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4
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1
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1
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1
1
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D-aspartate oxidase localisati ...
Sus scrofa
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2010
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7
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1
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1
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1
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712787
Takahashi
-
An active-site mutation enhanc ...
Vanrija humicola
J. Mol. Catal. B
61
235-240
2009
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1
1
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5
1
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1
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5
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11
-
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1
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1
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-
15
-
5
1
1
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-
5
1
-
-
-
-
-
-
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7
7
684387
Katane
Hyperactive mutants of mouse D ...
Mus musculus
Amino Acids
35
75-82
2008
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-
1
-
3
-
-
12
-
-
-
-
-
3
-
-
1
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1
12
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2
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1
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12
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1
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1
12
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2
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-
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686597
Huang
D-Aspartate and D-aspartate ox ...
Mus musculus
Exp. Eye Res.
86
704-709
2008
-
-
-
-
-
-
-
-
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4
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2
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1
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2
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1
-
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-
-
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-
-
-
-
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-
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673583
Katane
Caenorhabditis elegans has two ...
Caenorhabditis elegans
FEBS J.
274
137-149
2007
-
-
1
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-
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-
10
-
-
4
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3
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-
1
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-
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17
-
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10
-
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1
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1
1
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10
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4
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1
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-
-
17
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
684383
Katane
Molecular cloning of a cDNA en ...
Mus musculus
Amino Acids
32
69-78
2007
-
-
1
-
7
-
3
-
-
-
1
-
-
3
-
-
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-
2
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7
-
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2
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1
2
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7
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3
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1
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2
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7
-
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687440
Yamamoto
Functional and structural char ...
Sus scrofa
J. Biochem.
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2007
2
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1
-
-
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2
3
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4
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3
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1
-
-
2
2
-
3
1
-
-
-
3
1
-
1
1
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-
-
2
-
1
1
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-
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-
2
-
3
-
-
4
-
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-
1
-
2
2
-
3
1
-
-
-
3
1
-
1
-
-
-
-
-
-
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677271
Takahashi
Physiological role of D-aspart ...
Vanrija humicola
Yeast
22
1203-1212
2005
-
-
-
-
-
-
-
-
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1
-
3
-
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-
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1
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1
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1
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-
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-
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655928
Takahashi
Cloning and expression in Esch ...
Vanrija humicola
J. Biochem.
135
533-540
2004
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1
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2
3
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3
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6
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1
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1
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3
1
1
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2
3
1
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1
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2
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3
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3
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1
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1
-
3
1
1
-
2
3
1
-
-
-
-
-
-
-
-
-
657350
Sarower
-
Distribution and substrate spe ...
Meretrix lusoria, Mizuhopecten yessoensis, Mytilus galloprovincialis, Octopus vulgaris, Penaeus japonicus, Procambarus clarkii, Todarodes pacificus, Turbo cornutus
Science Asia
30
335-340
2004
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-
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-
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8
-
8
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14
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16
-
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-
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-
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-
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-
-
-
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8
-
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-
-
14
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656415
Sarower
Distribution and characteristi ...
Chaunax fimbriatus, Cololabis saira, Cyprinus carpio, Dentex tumifrons, Lateolabrax japonicus, Oncorhynchus keta, Oncorhynchus masou, Oncorhynchus mykiss, Pagrus major, Paralichthys olivaceus, Plecoglossus altivelis, Pseudopleuronectes yokohamae, Sardinops melanostictus, Scomber japonicus, Thamnaconus tessellatus, Trachurus japonicus, Verasper variegatus
J. Exp. Zool. A
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2003
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-
-
-
-
1
1
17
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-
17
-
23
-
-
-
-
-
38
-
-
25
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
17
-
-
17
-
-
-
-
-
38
-
-
25
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391705
Sacchi
Engineering the substrate spec ...
Bos taurus
J. Biol. Chem.
277
27510-27516
2002
-
-
-
-
-
-
1
4
-
-
-
1
-
3
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391706
Zaar
Cellular and subcellular distr ...
Bos taurus, Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
J. Comp. Neurol.
450
272-282
2002
-
-
-
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3
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166
-
-
-
-
-
5
-
-
16
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
3
-
-
4
-
-
-
-
-
5
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391707
Negri
Purification of beef kidney D- ...
Bos taurus
Biochim. Biophys. Acta
1431
212-222
1999
-
-
1
-
-
-
1
10
-
-
3
1
-
3
-
-
1
-
-
3
1
-
11
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
10
-
-
3
1
-
-
-
1
-
3
1
-
11
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391708
Tedeschi
D-Aspartate oxidase is present ...
Bos taurus, Xenopus laevis
Comp. Biochem. Physiol. B
124
489-494
1999
-
-
-
-
-
-
2
-
-
-
1
2
-
7
-
-
2
-
-
6
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
2
-
-
-
2
-
6
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391709
Amery
C-terminal tripeptide Ser-Asn- ...
Homo sapiens
Biochem. J.
336
367-371
1998
-
1
1
-
-
-
-
-
1
-
-
1
-
3
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-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
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-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391710
Kera
-
D-Aspartate oxidase and free a ...
Carassius auratus langsdorfii, Cyprinus carpio, Oncorhynchus mykiss, Pagrus major, Seriola quinqueradiata
Comp. Biochem. Physiol. B
119
95-100
1998
-
-
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7
-
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9
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11
11
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24
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4
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-
-
-
-
-
4
-
-
-
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7
-
-
-
-
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9
-
-
-
-
-
11
11
-
24
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391711
Simonic
cDNA cloning and expression of ...
Bos taurus
Biochem. J.
322
729-735
1997
-
-
1
-
-
-
-
-
-
-
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1
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2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391712
Setoyama
Structural and functional char ...
Homo sapiens
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798-803
1997
-
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1
-
-
-
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2
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1
1
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1
-
-
2
-
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4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
1
1
-
-
-
1
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391713
Yamada
Purification and properties of ...
Vanrija humicola, Vanrija humicola UJ1
Biochim. Biophys. Acta
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153-158
1996
-
-
-
-
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3
3
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1
2
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6
-
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1
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1
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8
1
1
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-
-
1
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1
3
-
-
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-
-
1
-
-
-
-
3
3
3
-
-
1
2
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-
-
1
-
-
1
-
8
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391714
Tedeschi
Properties of the flavoenzyme ...
Octopus vulgaris
Biochim. Biophys. Acta
1207
217-222
1994
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-
-
-
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-
6
-
-
1
1
-
5
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7
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1
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1
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1
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6
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1
1
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-
7
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
391715
Wakayama
-
Isolation, enzyme production a ...
Fusarium sacchari
J. Ferment. Bioeng.
78
377-379
1994
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
4
-
1
-
1
-
1
-
1
1
-
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-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
391716
D'Aniello
Biological role of D-amino aci ...
Mus musculus, Octopus vulgaris, Rattus norvegicus
J. Biol. Chem.
268
26941-26949
1993
-
-
-
-
-
-
-
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-
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-
3
-
5
-
-
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-
-
6
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6
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3
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-
3
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3
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6
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391717
D'Aniello
Further study on the specifici ...
Bos taurus, Octopus vulgaris
Comp. Biochem. Physiol. B
105
731-734
1993
-
-
-
-
-
-
-
14
-
-
-
2
-
4
-
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-
-
-
2
-
-
13
-
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-
2
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2
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-
14
-
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2
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-
2
-
-
13
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
391718
Tedeschi
Chemical modification of funct ...
Bos taurus
Eur. J. Biochem.
205
127-132
1992
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-
-
-
-
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1
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2
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2
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3
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1
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1
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1
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2
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3
-
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-
-
-
-
-
-
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-
-
-
-
391719
Negri
-
Structural studies of beef kid ...
Bos taurus
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
179-187
1990
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-
-
-
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-
2
1
-
1
1
-
1
-
-
1
-
-
1
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-
5
-
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-
1
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1
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-
1
-
-
-
-
-
-
2
1
-
1
1
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-
1
-
1
-
-
5
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
391720
Tedeschi
-
Modification of substrate spec ...
Bos taurus
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
189-192
1990
-
-
-
-
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-
1
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1
-
1
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-
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-
1
-
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6
-
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1
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-
1
-
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1
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1
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-
1
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391721
Negri
The kinetic mechanism of beef ...
Bos taurus
J. Biol. Chem.
263
13557-13563
1988
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-
-
-
-
-
-
2
-
-
1
1
-
2
-
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-
-
2
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-
2
1
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-
-
2
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-
1
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-
1
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-
2
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1
1
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-
2
-
-
2
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
391722
Negri
D-Aspartate oxidase from beef ...
Bos taurus
J. Biol. Chem.
262
10026-10034
1987
-
-
-
-
-
-
-
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-
-
1
1
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2
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1
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3
1
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2
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1
1
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1
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3
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391723
Burns
Thiazolidine-2-carboxylate der ...
Bos taurus
Biochem. Biophys. Res. Commun.
125
1039-1045
1984
-
-
-
-
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4
-
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1
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2
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2
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4
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4
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1
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2
-
-
4
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
391724
Nasu
The mammalian enzyme which rep ...
Bos taurus
Biochim. Biophys. Acta
704
240-252
1982
-
-
-
-
-
-
-
-
-
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-
1
-
3
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-
1
1
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2
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1
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-
1
-
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-
1
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-
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-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391725
Rinaldi
Oxidation of meso-diaminosucci ...
Bos taurus
Eur. J. Biochem.
117
635-638
1981
-
-
-
-
-
-
-
2
-
-
-
2
-
2
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2
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3
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1
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1
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2
-
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2
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2
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391726
Jaroszewicz
D-Asparatate oxidase in the th ...
Sus scrofa
Enzyme
20
80-89
1975
-
-
-
-
-
-
1
-
1
-
-
1
-
2
-
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1
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-
2
1
-
3
-
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-
1
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1
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-
1
-
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1
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-
1
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-
1
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1
-
2
1
-
3
-
-
-
-
-
1
-
-
-
-
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-
-
-
-
391727
Dixon
D-aspartate oxidase of kidney ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
146
54-76
1967
-
-
-
-
-
-
15
4
-
-
-
1
-
1
-
-
1
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-
1
1
-
3
-
-
-
-
-
2
1
1
-
2
-
-
-
-
-
-
-
-
-
-
15
2
4
-
-
-
1
-
-
-
1
-
1
1
-
3
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
391728
Still
-
On the prosthetic group of the ...
Oryctolagus cuniculus, Ovis aries, Sus scrofa
J. Biol. Chem.
182
585-589
1950
-
-
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1
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3
-
3
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2
-
1
6
-
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2
-
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-
2
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-
1
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3
-
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-
2
-
1
6
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-