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Information on EC 1.4.3.3 - D-amino-acid oxidase and Organism(s) Rattus norvegicus and UniProt Accession O35078
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1.4.3.3 D-amino-acid oxidaseIUBMB Comments
A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts on glycine.
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Word Map
- 1.4.3.3
- d-serine
-
schizophrenia
- peroxisomal
- flavin
- n-methyl-d-aspartate
- d-alanine
- catalase
- fad
- nmda
-
deamination
- benzoate
-
flavoenzyme
- flavoproteins
- racemase
- variabilis
-
l-amino
-
neurotransmission
- d-aspartate
- gracilis
-
co-agonist
- rhodotorula
- cephalosporin
-
glutamatergic
- urate
- d-proline
- d-ala
- d-ser
-
imino
-
antipsychotic
-
hypofunction
- d-methionine
- isoalloxazine
- acylase
-
fad-containing
- toruloides
- rhodosporidium
- d-glutamate
-
fad-dependent
- d-cysteine
-
kynurenic
- sulfurtransferase
- d-valine
- synthesis
- medicine
- d-leucine
- cerium
-
7-aminocephalosporanic
- d-tryptophan
- d-phenylalanine
- neuregulin
- 3-mercaptopyruvate
- sarcosine
- industry
- biotechnology
- analysis
- diagnostics
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
d-amino acid oxidase, d-amino-acid oxidase, hdaao, d-aao, rgdaao, tvdao, tvdaao, d-aminoacid oxidase, peg-dao, pkdaao, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-aminoacid oxidase
-
-
-
-
DAAO
DAMOX
-
-
-
-
DAO
ophio-amino-acid oxidase
-
-
-
-
oxidase, D-amino acid
-
-
-
-
DAAO
-
-
-
-
DAO
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-amino-acid:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts on glycine.
CAS REGISTRY NUMBER
COMMENTARY
9000-88-8
-
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-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
a D-amino acid + H2O + O2
a 2-oxo acid + NH3 + H2O2
-
D-amino-acid oxidase catalyzes the oxidative deamination of D-amino acids, stereoisomers of the naturally occurring L-amino acids
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
-
D-Dopa undergoes unidirectional chiral inversion and further suggest that D-Dopa is first oxidatively deaminated by DAAO to its alpha-keto acid and then transaminated by dopa transaminase to L-Dopa
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
high doses of D-serine attenuate both amphetamine-induced psychomotor activity and dopamine release and also improve performance in novel object recognition
-
-
?
additional information
?
-
D-amino acid oxidase is a flavoenzyme that catalyzes the oxidation of D-amino acids to the corresponding imino acids and hydrogen peroxide
-
-
?
additional information
?
-
-
D-amino acid oxidase is an enzyme catalyzing the strict stereospecificity the oxidative deamination of neutral and polar D-amino acids to alpha-keto acids, NH3 and hydrogen peroxide
-
-
?
additional information
?
-
-
the flavoenzyme catalyzes the oxidative deamination of neutral and basic D-amino acids to the corresponding 2-oxo acids and H2O2 with concomitant reduction of FAD
-
-
?
additional information
?
-
-
the enzyme interacts with the mammalian protein modulator pLG72
-
-
?
additional information
?
-
-
D-aspartate and glycine are no substrates
-
-
?
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
a D-amino acid + H2O + O2
a 2-oxo acid + NH3 + H2O2
-
D-amino-acid oxidase catalyzes the oxidative deamination of D-amino acids, stereoisomers of the naturally occurring L-amino acids
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
-
D-Dopa undergoes unidirectional chiral inversion and further suggest that D-Dopa is first oxidatively deaminated by DAAO to its alpha-keto acid and then transaminated by dopa transaminase to L-Dopa
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
high doses of D-serine attenuate both amphetamine-induced psychomotor activity and dopamine release and also improve performance in novel object recognition
-
-
?
additional information
?
-
-
D-amino acid oxidase is an enzyme catalyzing the strict stereospecificity the oxidative deamination of neutral and polar D-amino acids to alpha-keto acids, NH3 and hydrogen peroxide
-
-
?
additional information
?
-
-
the flavoenzyme catalyzes the oxidative deamination of neutral and basic D-amino acids to the corresponding 2-oxo acids and H2O2 with concomitant reduction of FAD
-
-
?
additional information
?
-
-
the enzyme interacts with the mammalian protein modulator pLG72
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine
-
MK-801, a drastic decline in the expression of DAO mRNA is observed in most brain areas 1 h after the MK-801 administration (1.6 mg/kg)
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
-
i.e. compound 8, a moderately potent inhibitor of rat DAAO in vitro, inhibits DAAO activity in kideny by 96% and in brain by 80% resulting in a significant elevation in both plasma and cerebrospinal fluid D-serine concentration. Compound 8 fails to significantly influence amphetamine-induced psychomotor activity, nucleus accumbens dopamine release, or a dizocilpine maleate-induced deficit in novel object recognition in rats
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
-
i.e. compound 8, very specific inhibitor of DAAO. Compound 8 at 200 mg/kg body weight inhibits rat kidney and cerebellar DAAO by approximately 96% and 80%, respectively. Effects after in vivo application, overview
additional information
-
negligible DAAO inhibition with muscimol, (S)-AMPA, 6-chloro-3-methoxybenzo[d]isoxazole, and 4,5,6,7-tetrahydrobenzo[d]isoxazol-3-ol
-
5-methylpyrazole-3-carboxylic acid
-
AS057278, selective D-amino acid oxidase inhibitor, 10 mg/kg
Sodium benzoate
-
competitive inhibitor, inhibits the development of mechanical allodynia, caused by enhanced enzyme expression, in the spinal cord, overview
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
morphine
the chronic treatment with morphine produces a slight but significant enhancement in the levels of DAO mRNA in the forebrain regions, the levels increases by 24%-102% in the striatum (87% increase), hippocampus (102%), and cortex (24%)
(+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine
-
MK-801, a dose-dependent elevation in the expression of DAO mRNA is observed in most brain areas 4 h after the administration (1.6 mg/kg)
pLG72
-
i.e. DAOA or D-amino acid oxidase activator, interacts with and activates the enzyme
-
additional information
no significant change in the protein expression of DAO is observed after administration of morphine for 30 days in the diencephalon, midbrain, pons medulla, and cerebellum
-
additional information
-
L5/L6 spinal nerve ligation in the lumbar spinal cord increases the enzyme activity with an increase in neuropathic pain, mechanical allodynia
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003081
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00847
3-hydroxy-5-methylquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000215
3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00004
5-chloro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000004
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00005
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.003665
5-ethyl-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000196
5-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000308
6-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00416
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.001445
7-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00015
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00224
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00799
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00014
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00872
8-chloro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00018
8-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.0002
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000424
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
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
-
DAO is restricted to the lower brainstem, cerebellum and spinal cord, decreasing levels in the midbrain, the cortex and hippocampus
-
D-amino acid oxidase is localized in the transitional cells, which are parasensory cells located between the sensory epithelium and the dark cells
additional information
in choroid plexus epithelial cells, glial cells of pons, medulla oblongata, and especially in Bergmann glia of cerebellum
-
in lower brain stem and cerebellum, as well as type-1 astrocytes from cerebral cortex and the cerebellum
-
D-amino-acid oxidase is involved in D-serine-induced nephrotoxicity
additional information
in situ hybridization and immunohistochemic determination
additional information
-
D-serine occurs in the cerebral cortex, hippocampus, anterior olfactory nucleus, olfactory tubercle, and amygdale, D-serine tissue distribution, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
D-serine is synthesized from L-serine by serine racemase and degraded by D-amino acid oxidase in neurons, overview
physiological function
additional information
-
metabolism of extracellular D-serine and effects of D-serine metabolites with pathophysiological role of DAO, overexpression of DAO in astroglial cells induces the enhanced cytotoxicity, reaction product beta-hydroxypyruvate also induces cell death, comprising apoptosis, in the astroglial cell, but not in the other cells derived from liver and kidney, overview
physiological function
-
D-amino acid oxidase is an enzyme catalyzing oxidative deamination of neutral and polar D-amino acids. It plays a role in neuropathic pain, in spinal nerve ligation-induced mechanical allodynia, which is specifically blocked by sodium benzoate
physiological function
-
spinal D-amino acid oxidase contributes to the pathogenesis of hyperalgesia
physiological function
-
DAO is associated with schizophrenia. DAO modulates neurotransmission by metabolizing the D-serine, that binds to the coagonist-binding site of N-methyl-D-aspartate subtype of glutamate receptors and enhances the neurotransmission. DAO might be involved in D-serine-induced nephrotoxicity only in rats
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). OXDA_RAT
346
0
38820
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme with bound inhibitor 3-hydroxyquinolin-2(1H)-one, X-ray diffraction structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of a mutant rat strain LEA/SENDAI lacking D-amino-acid oxidase
additional information
-
development of an implantable D-serine biosensor for in vivo monitoring using mammalian D-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode, method evaluation, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L5/L6 spinal nerve ligation in the lumbar spinal cord increases the enzyme expression correlated with an increase in neuropathic pain, mechanical allodynia
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
th enzyme is useful for measurement of D-serine contents in the brain via an implantable D-serine biosensor for in vivo monitoring
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dememes, D.; Mothet, J.P.; Nicolas, M.T.
Cellular distribution of d-serine, serine racemase and d-amino acid oxidase in the rat vestibular sensory epithelia
Neuroscience
137
991-997
2006
Rattus norvegicus
Maekawa, M.; Okamura, T.; Kasai, N.; Hori, Y.; Summer, K.H.; Konno, R.
D-amino-acid oxidase is involved in D-serine-induced nephrotoxicity
Chem. Res. Toxicol.
18
1678-1682
2005
Rattus norvegicus
Wu, M.; Zhou, X.J.; Konno, R.; Wang, Y.X.
D-dopa is unidirectionally converted to L-dopa by D-amino acid oxidase, followed by dopa transaminase
Clin. Exp. Pharmacol. Physiol.
33
1042-1046
2006
Rattus norvegicus
Tanaka, H.; Yamamoto, A.; Ishida, T.; Horiike, K.
Simultaneous measurement of D-serine dehydratase and d-amino acid oxidase activities by the detection of 2-oxo-acid formation with reverse-phase high-performance liquid chromatography
Anal. Biochem.
362
83-88
2007
Gallus gallus, Rattus norvegicus
Hashimoto, A.; Yoshikawa, M.; Andoh, H.; Yano, H.; Matsumoto, H.; Kawaguchi, M.; Oka, T.; Kobayashi, H.
Effects of MK-801 on the expression of serine racemase and D-amino acid oxidase mRNAs and on the D-serine levels in rat brain
Eur. J. Pharmacol.
555
17-22
2007
Rattus norvegicus
Pollegioni, L.; Piubelli, L.; Sacchi, S.; Pilone, M.S.; Molla, G.
Physiological functions of D-amino acid oxidases: from yeast to humans
Cell. Mol. Life Sci.
64
1373-1394
2007
Chlorella vulgaris, Rattus norvegicus (O35078), Sus scrofa (P00371), Homo sapiens (P14920), Homo sapiens, Mus musculus (P18894), Rhodotorula toruloides (P80324), Cyprinus carpio (Q6TGN2), Trigonopsis variabilis (Q99042), [Candida] boidinii (Q9HGY3)
Adage, T.; Trillat, A.C.; Quattropani, A.; Perrin, D.; Cavarec, L.; Shaw, J.; Guerassimenko, O.; Giachetti, C.; Greco, B.; Chumakov, I.; Halazy, S.; Roach, A.; Zaratin, P.
In vitro and in vivo pharmacological profile of AS057278, a selective D-amino acid oxidase inhibitor with potential anti-psychotic properties
Eur. Neuropsychopharmacol.
18
200-214
2008
Rattus norvegicus, Homo sapiens (P14920), Homo sapiens
Ferraris, D.; Duvall, B.; Ko, Y.S.; Thomas, A.G.; Rojas, C.; Majer, P.; Hashimoto, K.; Tsukamoto, T.
Synthesis and biological evaluation of D-amino acid oxidase inhibitors
J. Med. Chem.
51
3357-3359
2008
Rattus norvegicus
Yoshikawa, M.; Shinomiya, T.; Takayasu, N.; Tsukamoto, H.; Kawaguchi, M.; Kobayashi, H.; Oka, T.; Hashimoto, A.
Long-term treatment with morphine increases the D-serine content in the rat brain by regulating the mRNA and protein expressions of serine racemase and D-amino acid oxidase
J. Pharmacol. Sci.
107
270-276
2008
Rattus norvegicus (O35078)
Konno, R.; Okamura, T.; Kasai, N.; Summer, K.H.; Niwa, A.
Mutant rat strain lacking D-amino-acid oxidase
Amino Acids
37
367-375
2009
Rattus norvegicus
Williams, M.
Commentary: genome-based CNS drug discovery: D-amino acid oxidase (DAAO) as a novel target for antipsychotic medications: progress and challenges
Biochem. Pharmacol.
78
1360-1365
2009
Homo sapiens, Rattus norvegicus
Duplantier, A.J.; Becker, S.L.; Bohanon, M.J.; Borzilleri, K.A.; Chrunyk, B.A.; Downs, J.T.; Hu, L.Y.; El-Kattan, A.; James, L.C.; Liu, S.; Lu, J.; Maklad, N.; Mansour, M.N.; Mente, S.; Piotrowski, M.A.; Sakya, S.M.; Sheehan, S.; Steyn, S.J.; Strick, C.A.; Williams, V.A.; Zhang, L.
Discovery, SAR, and pharmacokinetics of a novel 3-hydroxyquinolin-2(1H)-one series of potent D-amino acid oxidase (DAAO) inhibitors
J. Med. Chem.
52
3576-3585
2009
Rattus norvegicus, Homo sapiens (P14920), Homo sapiens
Ono, K.; Shishido, Y.; Park, H.K.; Kawazoe, T.; Iwana, S.; Chung, S.P.; Abou El-Magd, R.M.; Yorita, K.; Okano, M.; Watanabe, T.; Sano, N.; Bando, Y.; Arima, K.; Sakai, T.; Fukui, K.
Potential pathophysiological role of D-amino acid oxidase in schizophrenia: immunohistochemical and in situ hybridization study of the expression in human and rat brain
J. Neural Transm.
116
1335-1347
2009
Homo sapiens, Rattus norvegicus (O35078)
Smith, S.M.; Uslaner, J.M.; Yao, L.; Mullins, C.M.; Surles, N.O.; Huszar, S.L.; McNaughton, C.H.; Pascarella, D.M.; Kandebo, M.; Hinchliffe, R.M.; Sparey, T.; Brandon, N.J.; Jones, B.; Venkatraman, S.; Young, M.B.; Sachs, N.; Jacobson, M.A.; Hutson, P.H.
The behavioral and neurochemical effects of a novel D-amino acid oxidase inhibitor compound 8 [4H-thieno [3,2-b]pyrrole-5-carboxylic acid] and D-serine
J. Pharmacol. Exp. Ther.
328
921-930
2009
Homo sapiens, Rattus norvegicus
Zhao, W.J.; Gao, Z.Y.; Wei, H.; Nie, H.Z.; Zhao, Q.; Zhou, X.J.; Wang, Y.X.
Spinal D-amino acid oxidase contributes to neuropathic pain in rats
J. Pharmacol. Exp. Ther.
332
248-254
2009
Rattus norvegicus
Zain, Z.M.; ONeill, R.D.; Lowry, J.P.; Pierce, K.W.; Tricklebank, M.; Dewa, A.; Ab Ghani, S.
Development of an implantable D-serine biosensor for in vivo monitoring using mammalian D-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode
Biosens. Bioelectron.
25
1454-1459
2010
Rattus norvegicus
Konno, R.; Hamase, K.; Maruyama, R.; Zaitsu, K.
Mutant mice and rats lacking D-amino acid oxidase
Chem. Biodivers.
7
1450-1458
2010
Mus musculus, Rattus norvegicus
Chung, S.P.; Sogabe, K.; Park, H.K.; Song, Y.; Ono, K.; Abou El-Magd, R.M.; Shishido, Y.; Yorita, K.; Sakai, T.; Fukui, K.
Potential cytotoxic effect of hydroxypyruvate produced from D-serine by astroglial D-amino acid oxidase
J. Biochem.
148
743-753
2010
Rattus norvegicus
Frattini, L.F.; Piubelli, L.; Sacchi, S.; Molla, G.; Pollegioni, L.
Is rat an appropriate animal model to study the involvement of D-serine catabolism in schizophrenia? Insights from characterization of D-amino acid oxidase
FEBS J.
278
4362-4373
2011
Rattus norvegicus
Luks, L.; Sacchi, S.; Pollegioni, L.; Dietrich, D.R.
Novel insights into renal D-amino acid oxidase accumulation propiverine changes DAAO localization and peroxisomal size in vivo
Arch. Toxicol.
91
427-437
2017
Rattus norvegicus
Xie, D.; Lu, J.; Xie, J.; Cui, J.; Li, T.F.; Wang, Y.C.; Chen, Y.; Gong, N.; Li, X.Y.; Fu, L.; Wang, Y.X.
Discovery and analgesic evaluation of 8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione as a novel potent D-amino acid oxidase inhibitor
Eur. J. Med. Chem.
117
19-32
2016
Homo sapiens, Rattus norvegicus, Sus scrofa
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