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3,4-dihydroxy-D-phenylalanine + H2O + O2
3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
-
-
-
?
alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
?
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
D-cycloserine + H2O + O2
? + NH3 + H2O2
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
-
-
?
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvic acid + NH3 + H2O2
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-kynurenine + H2O + O2
kynurenate + NH3 + H2O2
-
-
-
?
D-kynurenine + H2O + O2
kynurenic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
D-Pro + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
D-serine + H2O + O2
2-oxo-3-hydroxypropanoate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
D-serine + H2O + O2
?
-
-
-
?
D-serine + H2O + O2
oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
D-tyrosine + H2O + O2
3-(4-hydroxyphenyl)pyruvate + NH3 + H2O2
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
Gly + H2O + O2
acetate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
L-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
-
-
?
N-acetyl-D-alanine + H2O + O2
pyruvate + aminoacetate + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
?
tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
?
additional information
?
-
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
-
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
-
best substrate
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
-
-
-
-
?
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvic acid + NH3 + H2O2
the maximal velocity for oxidation of D-DOPA is much greater than for D-serine
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
best substrate
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
D-serine, an endogenous agonist of the N-methyl-D-aspartate, NMDA, receptors, is effective in the treatment of schizophrenia. However, orally administered D-serine is metabolized substantially by D-amino acid oxidase diminishing its oral bioavailability
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
metabolizaation of the N-methyl D-aspartate receptor co-agonist
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
the apoprotein form of hDAAO binds the substrate D-serine, which increases FAD binding thus increasing the amount of active holoenzyme in solution
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
low catalytic efficiency and substrate affinity on the physiological substrate D-serine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
-
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
additional information
?
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
-
DAAO is a catabolic flavoenzyme that catalyzes the oxidative deamination of D-amino acids to the corresponding a-keto acids, hydrogen peroxide, and ammonia. DAAO is strictly specific for D-isomers of amino acids
-
-
?
additional information
?
-
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
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
?
-
-
hDAAO exhibits optimal activity toward neutral D-amino acids and marginal activity toward basic ones, while acidic D-amino acids are not oxidized, structure-function relationship analysis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
-
-
?
additional information
?
-
DAAO interacts with its physiological partner pLG72, the interaction is not inhibited by benzoate and chlorpromazine
-
-
?
additional information
?
-
-
DAAO interacts with its physiological partner pLG72, the interaction is not inhibited by benzoate and chlorpromazine
-
-
?
additional information
?
-
comparison of the kinetics of trypsin cleavage of hDAAO in the presence of various ligands, overview
-
-
?
additional information
?
-
-
comparison of the kinetics of trypsin cleavage of hDAAO in the presence of various ligands, overview
-
-
?
additional information
?
-
DAAO is mainly active on neutral, hydrophobic and slightly polar D-amino acids and shows a preference for aromatic amino acids
-
-
-
additional information
?
-
-
DAAO is mainly active on neutral, hydrophobic and slightly polar D-amino acids and shows a preference for aromatic amino acids
-
-
-
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([4-[(3,4-dichloro-5-methyl-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
([4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
([4-[(4,5-dichloro-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
([4-[(4-bromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
1,4-dihydropyrrolo[3,2-c]pyrazole-5-carboxylic acid
-
1H-indole-2-carboxylic acid
-
1H-pyrrole-2-carboxylic acid
-
2,3-dimethyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
-
-
2-(2,4-dichlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-(3,3-dimethylbutyl)-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
-
-
2-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-(hydroxymethyl)-5-((4-methoxybenzyl)oxy)-4H-pyran-4-one
-
2-benzyl-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
-
-
2-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-chloro-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
2-phenyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-[(3,4-dichlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[(4-chlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[(4-fluorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[(benzyloxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[2-(1H-benzimidazol-1-yl)ethyl]-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
-
-
2-[[(1Z)-1-chloroprop-1-en-1-yl]sulfanyl]prop-2-enoic acid
-
-
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
2-[[(4-chlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
2-[[(4-fluorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
2-{[(3,4-dichlorophenyl)sulfanyl]methyl}-5-hydroxy-4H-pyran-4-one
-
-
3,3-dibromo-4-chloro-5-fluoro-2,3-dihydro-1H-pyrrolo[2,3-b]pyridine
-
3-(2-phenylethyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-(7-hydroxy-2-oxo-4-phenyl-2H-1-benzopyran-6-yl)propanoic acid
-
-
3-(benzylsulfanyl)-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-(hydroxymethyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-benzyl-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-cyano-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
3-hydroxy-1,5-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,7-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-2H-1-benzopyran-2-one
3-hydroxy-4-methylquinolin-2(1H)-one
-
3-hydroxy-5-(2-phenylethyl)pyridin-2(1H)-one
-
-
3-hydroxy-5-methylpyridin-2(1H)-one
-
-
3-hydroxy-5-methylquinolin-2(1H)-one
-
3-hydroxy-6-methylquinolin-2(1H)-one
-
3-hydroxy-7-methylquinolin-2(1H)-one
-
3-hydroxy-8-methylquinolin-2(1H)-one
-
3-hydroxypyridin-2(1H)-one
-
-
3-hydroxyquinolin-2(1H)-one
3-hydroxyquinolin-2-(1H)-one
-
-
3-hydroxyquinolin-2-one
-
-
3-hydroxyquinoline-2-(1H)-one
-
very potent inhibitor
3-methyl-1H-pyrazole-5-carboxylic acid
-
-
3-pyridin-3-yl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-thiophencarboxylic acid
-
-
3-[(cyclohexylmethyl)sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(1,2-benzoxazol-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(2H-1,3-benzodioxol-5-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(3,4-dichlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(4-chlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(4-tert-butylphenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(6-fluoronaphthalen-2-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[([1,1'-biphenyl]-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[([1,1'-biphenyl]-4-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
4,5-dichlorofuran-2-carboxylic acid
-
4,5-dichlorothiophene-2-carboxylic acid
-
-
4,5-dimethylthiophene-2-carboxylic acid
-
-
4,6-difluoro-1-hydroxy-1,3-dihydro-2H-benzimidazol-2-one
-
-
4,6-difluoro-1-hydroxy-1H-benzo[d]imidazol-2(3H)-one
4-(difluoromethyl)thiophene-2-carboxylic acid
-
-
4-bromo-3-nitrobenzoate
there are two binding pockets of DAO to its inhibitor 4-bromo-3-nitrobenzoate, one is shared with substrate D-Ser and FAD, and the other is an cleft between the subunits of a DAO dimer
-
4-chloro-5-fluoro-1H-pyrrolo[2,3-b]pyridine-2,3-dione
-
4-hydroxy-6-(1-phenylethyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-(2-phenylethyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-(3-phenylpropyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-(phenoxymethyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-(3-methoxyphenyl)ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-(4-methoxyphenyl)ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-(7-hydroxy-2-oxo-4-phenyl-2H-1-benzopyran-6-yl)ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[2-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[3-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[4-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[7-hydroxy-4-(3-methoxyphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[7-hydroxy-4-(3-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[7-hydroxy-4-(4-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
-
-
4-methylthiophene-2-carboxylic acid
-
-
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-3-carboxylic acid
-
4H-furo[3,2-b]pyrrole-5-carboxylic acid
4H-pyrrolo[2,3-d][1,3]oxazole-5-carboxylic acid
-
4H-pyrrolo[2,3-d][1,3]thiazole-5-carboxylic acid
-
4H-pyrrolo[3,2-d][1,3]thiazole-5-carboxylic acid
-
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
-
i.e. compound 8, a moderately potent inhibitor of human DAAO in vitro
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
-
i.e. compound 8, very specific inhibitor of DAAO
4H-thieno[3,2-b]-pyrrole-5-carboxylic acid
-
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
5,6-dichloro-1,2-benzoxazol-3-ol
-
5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylic acid
-
-
5-(difluoromethyl)thiophene-2-carboxylic acid
-
-
5-(trifluoromethyl)thiophene-2-carboxylic acid
-
-
5-bromothiophene-2-carboxylic acid
-
-
5-chloro-3-hydroxypyridin-2(1H)-one
-
-
5-chloro-3-hydroxyquinolin-2(1H)-one
-
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
-
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
-
5-chloro-benzo[d]isoxazol-3-ol
-
-
5-chlorothiophene-2-carboxylic acid
-
-
5-ethyl-3-hydroxyquinolin-2(1H)-one
-
5-fluoro-3-hydroxyquinolin-2(1H)-one
-
5-fluorothiophene-2-carboxylic acid
-
-
5-hydroxy-2-(2-phenylethyl)-4H-pyran-4-one
-
5-hydroxy-2-(methoxymethyl)-4H-pyran-4-one
-
5-hydroxy-2-(phenoxymethyl)-4H-pyran-4-one
-
5-hydroxy-2-[(naphthalen-1-yloxy)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(naphthalen-2-yloxy)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(phenylsulfanyl)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(pyridin-3-yloxy)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(pyrimidin-2-ylsulfanyl)methyl]-4H-pyran-4-one
-
5-hydroxy-3-(2-phenylethyl)-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-3-(3-phenylpropyl)-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-3-[(2-phenylethyl)sulfanyl]-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-3-[[(4-iodophenyl)methyl]sulfanyl]-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-4-methyl-3-[(naphthalen-1-yl)methyl]pyridine-2,6(1H,3H)-dione
-
-
5-methylpyrazole-3-carboxylic acid
5-methylthiophene-2-carboxylic acid
-
-
6-(2-cyclohexylethyl)-4-hydroxypyridazin-3(2H)-one
-
-
6-(3,3-dimethylbutyl)-4-hydroxypyridazin-3(2H)-one
-
-
6-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-chloro-1,2-benzisoxazol-3-ol
-
6-chloro-1,2-benzoxazol-3-ol
-
-
6-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-chloro-3-hydroxyquinolin-2(1H)-one
-
6-chlorobenzo[d]isoxazol-3-ol
6-chlorobenzo[d]isoxazole-3-ol
-
-
6-cyclohexyl-4-hydroxypyridazin-3(2H)-one
-
-
6-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-fluoro-3-hydroxyquinolin-2(1H)-one
-
6-hydroxy-2-(2-(naphthalen-1-yl)ethyl)-1,2,4-triazine-3,5-(2H,4H)-dione
-
-
6-hydroxy-2-(2-phenylethyl)-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-(3-methylbutyl)-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-(3-phenylpropyl)-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-methyl-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-phenyl-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[(naphthalen-1-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[(naphthalen-2-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[2-(1H-pyrazol-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[2-(1H-pyrrolo[2,3-b]pyridin-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[2-(pyridin-2-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-phenethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-[(E)-2-(4-chlorophenyl)vinyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(2-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(3,5-difluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(3,5-dimethoxyphenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(3-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(4-chlorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(4-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-[3,5-bis(trifluoromethyl)phenyl]ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-[4-(3-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-[4-(4-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6H-thieno[2,3-b]pyrrole-5-carboxylic acid
-
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-3-hydroxyquinolin-2(1H)-one
-
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-ethyl-3-hydroxyquinolin-2(1H)-one
-
7-fluoro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-fluoro-3-hydroxyquinolin-2(1H)-one
-
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-hydroxypyrido[2,3-b]pyrazin-6(5H)-one
-
7-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
potent inhibitor
8-chloro-3-hydroxyquinolin-2(1H)-one
-
8-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethyl-3-hydroxyquinolin-2(1H)-one
-
8-fluoro-3-hydroxyquinolin-2(1H)-one
-
8-isopropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
imidazo[1,2-a]pyridine-6-carboxylic acid
-
-
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
-
-
pLG72
-
acts as a negative effector of DAAO
-
quinoxaline-2,3-dione
-
-
thiophene-2-carboxylic acid
-
trifluoro-D-alanine
-
pseudo-substrate
[[4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl](methyl)amino]acetic acid
100% inhibition at 0.02 mM
-
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
-
3-hydroxy-2H-1-benzopyran-2-one
-
3-hydroxy-2H-1-benzopyran-2-one
-
-
3-hydroxyquinolin-2(1H)-one
-
3-hydroxyquinolin-2(1H)-one
-
-
4,6-difluoro-1-hydroxy-1H-benzo[d]imidazol-2(3H)-one
-
4,6-difluoro-1-hydroxy-1H-benzo[d]imidazol-2(3H)-one
-
-
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
-
-
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
-
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
-
-
4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
-
5-methylpyrazole-3-carboxylic acid
AS057278, selective D-amino acid oxidase inhibitor
5-methylpyrazole-3-carboxylic acid
-
i.e. AS057278
5-methylpyrazole-3-carboxylic acid
-
-
6-chlorobenzo[d]isoxazol-3-ol
-
competitive
6-chlorobenzo[d]isoxazol-3-ol
-
-
6-chlorobenzo[d]isoxazol-3-ol
-
6-chlorobenzo[d]isoxazol-3-ol
-
-
6-chlorobenzo[d]isoxazol-3-ol
a decrease in protein fluorescence is observed at increasing 6-chlorobenzo[d]isoxazol-3-ol concentrations
benzoate
-
-
benzoate
a classical substrate-competitive inhibitor, effect of benzoate on the FAD-binding process to hDAAO apoprotein
benzoate
-
competitive inhibitor
benzoate
a decrease in protein fluorescence is observed at increasing concentrations, with a biphasic change
chlorpromazine
-
chlorpromazine
competitive versus cofactor FAD
D-serine
-
-
Sodium benzoate
-
inhibits the enzyme activity by by impeding the interaction of the enzyme with the flavin prosthetic group
additional information
benzoate and CPZ similarly modify the short-term cellular D-serine concentration but affect the cellular concentration of hDAAO differently
-
additional information
-
benzoate and CPZ similarly modify the short-term cellular D-serine concentration but affect the cellular concentration of hDAAO differently
-
additional information
identification of inhibitors by a structure based virtual screening campaign based on the X-ray structures of DAAO complexes where larger ligands shift the loop (lid opening) covering the native binding site followed by the in vitro test. Compounds bind to the active site with a salt-bridge. Displacement of and interaction with the loop covering the active site contributes significantly to the activity of the most potent compounds
-
additional information
not inhibitory: N-acetyl-cysteine at 10 mM. No change in protein fluorescence is observed with glycine (up to 50mM), ATP (up to 20mM), NMDA (up to 50mM), or D-glutamate (up to 50mM)
-
additional information
-
not inhibitory: N-acetyl-cysteine at 10 mM. No change in protein fluorescence is observed with glycine (up to 50mM), ATP (up to 20mM), NMDA (up to 50mM), or D-glutamate (up to 50mM)
-
additional information
synthesis of inhibitors that interact with loop 218-224 at the top of the binding pocket and open the lid over the active site of DAAO. The DAAO inhibitors show low nanomolar activity and low sensitivity to the substituents investigated. The interactions of the linker connecting the pendant aromatic moiety and the acidic headgroup with the enzyme are crucial for achieving significant inhibitory activity
-
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Acidosis
Some aspects of proximal tubular sodium chloride reabsorption in Necturus kidney.
Alzheimer Disease
Benzoate, a D-Amino Acid Oxidase Inhibitor, for the Treatment of Early-Phase Alzheimer Disease: A Randomized, Double-Blind, Placebo-Controlled Trial.
Alzheimer Disease
Brain Activity of Benzoate, a D-Amino Acid Oxidase Inhibitor, in Patients With Mild Cognitive Impairment in a Randomized, Double-Blind, Placebo Controlled Clinical Trial.
Alzheimer Disease
Effect of Sodium Benzoate on Cognitive Function Among Patients With Behavioral and Psychological Symptoms of Dementia: Secondary Analysis of a Randomized Clinical Trial.
Alzheimer Disease
Precision Medicine of Sodium Benzoate for the Treatment of Behavioral and Psychological Symptoms of Dementia (BPSD).
Alzheimer Disease
Sodium benzoate for the treatment of behavioral and psychological symptoms of dementia (BPSD): A randomized, double-blind, placebo-controlled, 6-week trial.
Amyotrophic Lateral Sclerosis
Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase.
Amyotrophic Lateral Sclerosis
Insights into the role of d-amino acid oxidase mutations in amyotrophic lateral sclerosis.
Amyotrophic Lateral Sclerosis
Mechanistic insights into the loss-of-function mechanisms of rare human D-amino acid oxidase variants implicated in amyotrophic lateral sclerosis.
Amyotrophic Lateral Sclerosis
Pathogenic effects of amyotrophic lateral sclerosis-linked mutation in D-amino acid oxidase are mediated by D-serine.
Amyotrophic Lateral Sclerosis
Protein-RNA Networks Regulated by Normal and ALS-Associated Mutant HNRNPA2B1 in the Nervous System.
Anemia
Rat liver D-amino acid oxidase activity in iron deficiency anemia.
Anemia, Iron-Deficiency
Rat liver D-amino acid oxidase activity in iron deficiency anemia.
Ataxia
Mice lacking D-amino acid oxidase activity display marked attenuation of stereotypy and ataxia induced by MK-801.
Bone Neoplasms
Contributions of spinal D-amino acid oxidase to bone cancer pain.
Bone Neoplasms
Down-regulation of spinal D-amino acid oxidase expression blocks formalin-induced tonic pain.
Brain Neoplasms
Induction of cytotoxic oxidative stress by D-alanine in brain tumor cells expressing Rhodotorula gracilis D-amino acid oxidase: a cancer gene therapy strategy.
Carcinoma
Peroxisomal enzymes in normal and tumoral human breast.
Carcinoma, Hepatocellular
Functional interactions between oxidative stress, membrane Na(+) permeability, and cell volume in rat hepatoma cells.
Carcinoma, Hepatocellular
[Distribution, after differential centrifugation, of acid hydrolases, catalase, D-amino acid oxidase and urate oxidase in various Morris hepatomas]
Cardiomyopathy, Dilated
Chemogenetic generation of hydrogen peroxide in the heart induces severe cardiac dysfunction.
Cardiomyopathy, Dilated
Reversal of heart failure in a chemogenetic model of persistent cardiac redox stress.
d-amino-acid oxidase deficiency
d-Amino acid oxidase deficiency is caused by a large deletion in the Dao gene in LEA rats.
Dementia
A Post-hoc Study of D-Amino Acid Oxidase in Blood as an Indicator of Post-stroke Dementia.
Diabetes Mellitus, Experimental
Influence of insulin status on extra-mitochondrial oxygen metabolism in the rat.
Diabetes Mellitus, Experimental
Xanthine oxidase and D-amino-acid oxidase in fatty liver and alloxan diabetes.
Diabetic Retinopathy
Overexpression of D-amino acid oxidase prevents retinal neurovascular pathologies in diabetic rats.
Fatty Liver
Xanthine oxidase and D-amino-acid oxidase in fatty liver and alloxan diabetes.
Foot-and-Mouth Disease
Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli.
Glioblastoma
Characterization of human DAAO variants potentially related to an increased risk of schizophrenia.
Glioblastoma
Evidence for the interaction of d-amino acid oxidase with pLG72 in a glial cell line.
Glioblastoma
Identification of DNA-binding proteins that interact with the 5'-flanking region of the human d-amino acid oxidase gene by pull-down assay coupled with two-dimensional gel electrophoresis and mass spectrometry.
Glioblastoma
pLG72 modulates intracellular D-serine levels through its interaction with D-amino acid oxidase: effect on schizophrenia susceptibility.
Glioblastoma
Substitution of Arginine 120 in Human D-Amino Acid Oxidase Favors FAD-Binding and Nuclear Mistargeting.
Glioblastoma
The degradation (by distinct pathways) of human D-amino acid oxidase and its interacting partner pLG72--two key proteins in D-serine catabolism in the brain.
Glioma
D-amino acid oxidase gene therapy sensitizes glioma cells to the antiglycolytic effect of 3-bromopyruvate.
Glioma
D-Serine metabolism in C6 glioma cells: Involvement of alanine-serine-cysteine transporter (ASCT2) and serine racemase (SRR) but not D-amino acid oxidase (DAO).
Granulomatous Disease, Chronic
PEGylated D-amino acid oxidase restores bactericidal activity of neutrophils in chronic granulomatous disease via hypochlorite.
Heart Failure
Reversal of heart failure in a chemogenetic model of persistent cardiac redox stress.
Hyperalgesia
Contributions of spinal D-amino acid oxidase to chronic morphine-induced hyperalgesia.
Hyperalgesia
Glycine inhibitory dysfunction turns touch into pain through astrocyte-derived d-serine.
Hyperalgesia
Spinal D-Serine Increases PKC-Dependent GluN1 Phosphorylation Contributing to the Sigma-1 Receptor-Induced Development of Mechanical Allodynia in a Mouse Model of Neuropathic Pain.
Hyperalgesia
WITHDRAWN: Spinal d-amino acid oxidase contributes to the pathogenesis of hyperalgesia in the rat formalin test.
Hyperoxaluria, Primary
Enzymological characterization of a feline analogue of primary hyperoxaluria type 2: a model for the human disease.
Hyperpigmentation
Evaluation of In Vitro Function by Subcellular Distribution of Lysosomal and Peroxisomal Protein in Saccharomyces cerevisiae.
Hypersensitivity
Benzoate and Sorbate Salts: A Systematic Review of the Potential Hazards of These Invaluable Preservatives and the Expanding Spectrum of Clinical Uses for Sodium Benzoate.
Hypersensitivity
Spinal D-amino acid oxidase contributes to mechanical pain hypersensitivity induced by sleep deprivation in the rat.
Hypersensitivity
Spinal mechanisms contributing to the development of pain hypersensitivity induced by sphingolipids in the rat.
Hyperthyroidism
The effects of postnatal hyper- and hypothyroidism on the development of D-amino acid oxidase in rat cerebellum and brain stem.
Hypokinesia
Glycine-Binding Site Stimulants of NMDA Receptors Alleviate Extrapyramidal Motor Disorders by Activating the Nigrostriatal Dopaminergic Pathway.
Hypothyroidism
The effects of postnatal hyper- and hypothyroidism on the development of D-amino acid oxidase in rat cerebellum and brain stem.
Infections
Protective Role of D-Amino Acid Oxidase Against Staphylococcus aureus infection.
Infections
Salmonella evades D-amino acid oxidase to promote infection in neutrophils.
Malnutrition
Hepatic and renal D-amino acid oxidase activities in the growing rat after ten days of protein undernutrition and refeeding.
Neoplasms
3-Bromopyruvate antagonizes effects of lactate and pyruvate, synergizes with citrate and exerts novel anti-glioma effects.
Neoplasms
An antibody-based enzymatic therapy for cancer treatment: The selective localization of D-amino acid oxidase to EDA fibronectin.
Neoplasms
D-Aminoacid oxidase and homogentisate oxygenase activities in the tumor bearing rats.
Neoplasms
Determination of D-amino acid oxidase activity in tumour cells.
Neoplasms
Enhancement of chemotherapeutic response of tumor cells by a heme oxygenase inhibitor, pegylated zinc protoporphyrin.
Neoplasms
Induction of cytotoxic oxidative stress by D-alanine in brain tumor cells expressing Rhodotorula gracilis D-amino acid oxidase: a cancer gene therapy strategy.
Neoplasms
Optimization of D-amino acid oxidase for low substrate concentrations--towards a cancer enzyme therapy.
Neoplasms
Oxidoreductase activities in normal rat liver, tumor-bearing rat liver, and hepatoma HC-252.
Neoplasms
Oxystress inducing antitumor therapeutics via tumor-targeted delivery of PEG-conjugated D-amino acid oxidase.
Neoplasms
PEG-DAAO conjugate: A promising tool for cancer therapy optimized by protein engineering.
Neoplasms
Peroxisomes in human colon carcinomas. A cytochemical and biochemical study.
Neoplasms
Preparation of enzymatically highly active pegylated-D-amino acid oxidase and its application to antitumor therapy.
Neoplasms
THE DETERMINATION OF THE TOTAL D-AMINO ACID CONTENT OF HUMAN TUMORS AND NORMAL TISSUES BY MEANS OF D-AMINO ACID OXIDASE.
Neoplasms
Total Flavones of Abelmoschus manihot Remodels Gut Microbiota and Inhibits Microinflammation in Chronic Renal Failure Progression by Targeting Autophagy-Mediated Macrophage Polarization.
Neoplasms
Tumor-targeted delivery of polyethylene glycol-conjugated D-amino acid oxidase for antitumor therapy via enzymatic generation of hydrogen peroxide.
Nervous System Diseases
Novel human D-amino acid oxidase inhibitors stabilize an active-site lid-open conformation.
Neuralgia
An integrated review on new targets in the treatment of neuropathic pain.
Neuralgia
Binding Residence Time through Scaled Molecular Dynamics: A Prospective Application to hDAAO Inhibitors.
Neuralgia
Down-regulation of spinal D-amino acid oxidase expression blocks formalin-induced tonic pain.
Neuralgia
Drug Therapy of Neuropathic Pain: Current Developments and Future Perspectives.
Neuralgia
PHARMACODYNAMIC EFFECTS OF A D-AMINO ACID OXIDASE INHIBITOR INDICATE A SPINAL SITE OF ACTION IN RAT MODELS OF NEUROPATHIC PAIN.
Neuralgia
Spinal D-Amino Acid Oxidase Contributes to Neuropathic Pain in Rats.
Neurobehavioral Manifestations
D-amino Acid oxidase inhibitors as a novel class of drugs for schizophrenia therapy.
Neurobehavioral Manifestations
Drug discovery strategies and the preclinical development of D-amino-acid oxidase inhibitors as antipsychotic therapies.
Neurobehavioral Manifestations
Lack of Effect of Sodium Benzoate at Reported Clinical Therapeutic Concentration on d-Alanine Metabolism in Dogs.
Neurodegenerative Diseases
P219L substitution in human D-amino acid oxidase impacts the ligand binding and catalytic efficiency.
Neurodegenerative Diseases
The role of D-serine and glycine as co-agonists of NMDA receptors in motor neuron degeneration and amyotrophic lateral sclerosis (ALS).
Peroxisomal Disorders
Pipecolic acid is oxidized by renal and hepatic peroxisomes. Implications for Zellweger's cerebro-hepato-renal syndrome (CHRS).
Polyuria
D-amino-acid oxidase is involved in D-serine-induced nephrotoxicity.
Renal Aminoacidurias
Lack of D-amino-acid oxidase activity causes a specific renal aminoaciduria in the mouse.
Renal Insufficiency
D-Amino acids in chronic renal failure and the effects of dialysis and urinary losses.
Reperfusion Injury
Production of hydrogen sulfide from d-cysteine and its therapeutic potential.
Sarcoma 180
Oxystress inducing antitumor therapeutics via tumor-targeted delivery of PEG-conjugated D-amino acid oxidase.
Sleep Deprivation
Spinal D-amino acid oxidase contributes to mechanical pain hypersensitivity induced by sleep deprivation in the rat.
Spinocerebellar Ataxias
Localization of the candidate gene D-amino acid oxidase outside the refined I-cM region of spinocerebellar ataxia 2.
Staphylococcal Infections
Protective Role of D-Amino Acid Oxidase Against Staphylococcus aureus infection.
Starvation
Dynamics of D-amino acid oxidase in kidney epithelial cells under amino acid starvation.
Stomach Neoplasms
D-amino acid oxidase (DAO) rare genetic missense variant p.Pro103Leu and gastric cancer.
Thymoma
An update on the genetics of schizophrenia.
Tuberculosis
Knockout of MRA_1916 in Mycobacterium tuberculosis H37Ra affects its growth, biofilm formation, survival in macrophages and in mice.
Tuberculosis
The Mycobacterium tuberculosis H37Ra gene MRA_1916 causes growth defects upon down-regulation.
Urinary Bladder, Overactive
Identification of d-amino acid oxidase and propiverine interaction partners and their potential role in the propiverine-mediated nephropathy.
Zellweger Syndrome
Histochemistry of peroxisomal enzyme activities: a tool in the diagnosis of Zellweger syndrome.
Zellweger Syndrome
The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases.
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0.0088
([4-[(3,4-dichloro-5-methyl-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.00039
([4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0052
([4-[(4,5-dichloro-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0067
([4-[(4-bromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.005
1,4-dihydropyrrolo[3,2-c]pyrazole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.000745
1H-indole-2-carboxylic acid
Homo sapiens
-
0.005
1H-pyrrole-2-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2,3-dimethyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-(2,4-dichlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.04
2-(3,3-dimethylbutyl)-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.005
2-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0051
2-benzyl-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.005
2-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-chloro-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-phenyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0005
2-[(3,4-dichlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0007
2-[(4-chlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0008
2-[(4-fluorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.02
2-[(benzyloxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.00044
2-[2-(1H-benzimidazol-1-yl)ethyl]-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00036
2-[[(1Z)-1-chloroprop-1-en-1-yl]sulfanyl]prop-2-enoic acid
Homo sapiens
pH 8.5, 23°C
-
0.0001
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
2-[[(4-chlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0003
2-[[(4-fluorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.005
3-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
3-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0001
3-(benzylsulfanyl)-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.005
3-(hydroxymethyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.00007
3-benzyl-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001426
3-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.001153
3-cyano-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.000128
3-hydroxy-1,5-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000032
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000784
3-hydroxy-1,7-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000008 - 0.000009
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
0.0173
3-hydroxy-4-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0000039
3-hydroxy-5-(2-phenylethyl)pyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.00014
3-hydroxy-5-methylpyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000016
3-hydroxy-5-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00275
3-hydroxy-6-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000197
3-hydroxy-7-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000038
3-hydroxy-8-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0015
3-hydroxypyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000004 - 0.0000069
3-hydroxyquinolin-2(1H)-one
0.000004
3-hydroxyquinolin-2-(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000043
3-hydroxyquinolin-2-one
Homo sapiens
-
at pH 8.2 and 37°C
0.000004
3-hydroxyquinoline-2-(1H)-one
Homo sapiens
-
at pH 7.0 and 25°C
0.005
3-pyridin-3-yl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0006
3-[(cyclohexylmethyl)sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
3-[[(1,2-benzoxazol-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00006
3-[[(2H-1,3-benzodioxol-5-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
3-[[(3,4-dichlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
3-[[(4-chlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-[[(4-tert-butylphenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
3-[[(6-fluoronaphthalen-2-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
3-[[([1,1'-biphenyl]-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00009
3-[[([1,1'-biphenyl]-4-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000343
4,5-dichlorofuran-2-carboxylic acid
Homo sapiens
-
0.00009
4,5-dichlorothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0073
4,5-dimethylthiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0013
4-(difluoromethyl)thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0000049
4-hydroxy-6-(1-phenylethyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000038
4-hydroxy-6-(2-phenylethyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000013
4-hydroxy-6-(3-phenylpropyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000022
4-hydroxy-6-(phenoxymethyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000021
4-hydroxy-6-[2-(3-methoxyphenyl)ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000029
4-hydroxy-6-[2-(4-methoxyphenyl)ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000112
4-hydroxy-6-[2-(7-hydroxy-2-oxo-4-phenyl-2H-1-benzopyran-6-yl)ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.0000084
4-hydroxy-6-[2-[2-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000024
4-hydroxy-6-[2-[3-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000012
4-hydroxy-6-[2-[4-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000073
4-hydroxy-6-[2-[7-hydroxy-4-(3-methoxyphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000052
4-hydroxy-6-[2-[7-hydroxy-4-(3-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000474
4-hydroxy-6-[2-[7-hydroxy-4-(4-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.0013
4-methylthiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000238
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-3-carboxylic acid
Homo sapiens
-
0.0000014 - 0.000141
4H-furo[3,2-b]pyrrole-5-carboxylic acid
0.005
4H-pyrrolo[2,3-d][1,3]oxazole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.000516
4H-pyrrolo[2,3-d][1,3]thiazole-5-carboxylic acid
Homo sapiens
-
0.004204
4H-pyrrolo[3,2-d][1,3]thiazole-5-carboxylic acid
Homo sapiens
-
0.000145
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
-
0.000145
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
Homo sapiens
-
-
0.000145 - 0.000245
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
0.0088
5-(difluoromethyl)thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.021
5-(trifluoromethyl)thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0013
5-bromothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000047
5-chloro-3-hydroxypyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000004
5-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000003
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000005
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00072
5-chlorothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000008
5-ethyl-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000008
5-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0014
5-fluorothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0005
5-hydroxy-2-(2-phenylethyl)-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.05
5-hydroxy-2-(methoxymethyl)-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0009
5-hydroxy-2-(phenoxymethyl)-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0009
5-hydroxy-2-[(naphthalen-1-yloxy)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0008
5-hydroxy-2-[(naphthalen-2-yloxy)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
5-hydroxy-2-[(phenylsulfanyl)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.003
5-hydroxy-2-[(pyridin-3-yloxy)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.004
5-hydroxy-2-[(pyrimidin-2-ylsulfanyl)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.00006
5-hydroxy-3-(2-phenylethyl)-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.004
5-hydroxy-3-(3-phenylpropyl)-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.04
5-hydroxy-3-[(2-phenylethyl)sulfanyl]-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
5-hydroxy-3-[[(4-iodophenyl)methyl]sulfanyl]-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000901 - 0.00091
5-methylpyrazole-3-carboxylic acid
0.0046
5-methylthiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0000047
6-(2-cyclohexylethyl)-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.00067
6-(3,3-dimethylbutyl)-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000507
6-chloro-1,2-benzisoxazol-3-ol
Homo sapiens
-
0.000155
6-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00011 - 0.00019
6-chlorobenzo[d]isoxazol-3-ol
0.0003
6-cyclohexyl-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000009
6-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0001
6-hydroxy-2-(2-(naphthalen-1-yl)ethyl)-1,2,4-triazine-3,5-(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00007
6-hydroxy-2-(2-phenylethyl)-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00026
6-hydroxy-2-(3-methylbutyl)-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.0017
6-hydroxy-2-(3-phenylpropyl)-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.0028
6-hydroxy-2-methyl-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.1
6-hydroxy-2-phenyl-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00005
6-hydroxy-2-[(naphthalen-1-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00022
6-hydroxy-2-[(naphthalen-2-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00033
6-hydroxy-2-[2-(1H-pyrazol-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00031
6-hydroxy-2-[2-(1H-pyrrolo[2,3-b]pyridin-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00076
6-hydroxy-2-[2-(pyridin-2-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00012
6-[(E)-2-(4-chlorophenyl)vinyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000002
6-[2-(2-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000015
6-[2-(3,5-difluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000013
6-[2-(3,5-dimethoxyphenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000014
6-[2-(3-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000027
6-[2-(4-chlorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000031
6-[2-(4-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000063
6-[2-[3,5-bis(trifluoromethyl)phenyl]ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000069
6-[2-[4-(3-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000119
6-[2-[4-(4-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000269
6H-thieno[2,3-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.0001
7-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00113
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.0226
7-ethyl-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00001
7-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00034
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.05
7-hydroxypyrido[2,3-b]pyrazin-6(5H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00023
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.00138
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.00021
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.000033
8-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0144
8-ethyl-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000003
8-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.016
benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.002
kojic acid
Homo sapiens
pH and temperature not specified in the publication
0.0078
thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
0.00049
[[4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl](methyl)amino]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
additional information
additional information
-
0.000008
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000009
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000004
3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0000069
3-hydroxyquinolin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000014
4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000141
4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.000141
4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
at pH 7.0 and 25°C
0.000145
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
at pH 7.0 and 25°C
0.000245
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.000901
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
-
0.00091
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
0.00091
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
at pH 7.0 and 25°C
0.00091
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
at pH 8.2 and 37°C
0.00018
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
at pH 7.0 and 25°C
0.000188
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
-
0.00019
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
pH and temperature not specified in the publication
additional information
additional information
Homo sapiens
IC50 with substrate D-aspartate, overview
-
additional information
additional information
Homo sapiens
-
IC50 with substrate D-aspartate, overview
-
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Raibekas, A.A.; Fukui, K.; Massey, V.
Design and properties of human D-amino acid oxidase with covalently attached flavin
Proc. Natl. Acad. Sci. USA
97
3089-3093
2000
Homo sapiens
brenda
Pilone, M.S.
D-Amino acid oxidase: new findings
Cell. Mol. Life Sci.
57
1732-1747
2000
Homo sapiens, Rhodotorula toruloides, Sus scrofa, Trigonopsis variabilis
brenda
Molla, G.; Sacchi, S.; Bernasconi, M.; Pilone, M.S.; Fukui, K.; Polegioni, L.
Characterization of human D-amino acid oxidase
FEBS Lett.
580
2358-2364
2006
Homo sapiens
brenda
Kawazoe, T.; Tsuge, H.; Pilone, M.S.; Fukui, K.
Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring
Protein Sci.
15
2708-2717
2006
Homo sapiens
brenda
Verrall, L.; Walker, M.; Rawlings, N.; Benzel, I.; Kew, J.N.; Harrison, P.J.; Burnet, P.W.
D-Amino acid oxidase and serine racemase in human brain: normal distribution and altered expression in schizophrenia
Eur. J. Neurosci.
26
1657-1669
2007
Homo sapiens
brenda
Corvin, A.; McGhee, K.A.; Murphy, K.; Donohoe, G.; Nangle, J.M.; Schwaiger, S.; Kenny, N.; Clarke, S.; Meagher, D.; Quinn, J.; Scully, P.; Baldwin, P.; Browne, D.; Walsh, C.; Waddington, J.L.; Morris, D.W.; Gill, M.
Evidence for association and epistasis at the DAOA/G30 and D-amino acid oxidase loci in an Irish schizophrenia sample
Am. J. Med. Genet. B Neuropsychiatr. Genet.
144B
949-953
2007
Homo sapiens
brenda
Halvey, P.J.; Hansen, J.M.; Johnson, J.M.; Go, Y.M.; Samali, A.; Jones, D.P.
Selective oxidative stress in cell nuclei by nuclear-targeted D-amino acid oxidase
Antioxid. Redox Signal.
9
807-816
2007
Homo sapiens
brenda
Kawazoe, T.; Tsuge, H.; Imagawa, T.; Aki, K.; Kuramitsu, S.; Fukui, K.
Structural basis of D-DOPA oxidation by D-amino acid oxidase: altersodiumtive pathway for dopamine biosynthesis
Biochem. Biophys. Res. Commun.
355
385-391
2007
Homo sapiens (P14920), Homo sapiens
brenda
Sparey, T.; Abeywickrema, P.; Almond, S.; Brandon, N.; Byrne, N.; Campbell, A.; Hutson, P.H.; Jacobson, M.; Jones, B.; Munshi, S.; Pascarella, D.; Pike, A.; Prasad, G.S.; Sachs, N.; Sakatis, M.; Sardana, V.; Venkatraman, S.; Young, M.B.
The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors
Bioorg. Med. Chem. Lett.
18
3386-3391
2008
Homo sapiens (P14920)
brenda
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)
brenda
Kawazoe, T.; Park, H.K.; Iwana, S.; Tsuge, H.; Fukui, K.
Human D-amino acid oxidase: an update and review
Chem. Rec.
7
305-315
2007
Homo sapiens
brenda
Pollegioni, L.; Sacchi, S.; Caldinelli, L.; Boselli, A.; Pilone, M.S.; Piubelli, L.; Molla, G.
Engineering the properties of D-amino acid oxidases by a rational and a directed evolution approach
Curr. Protein Pept. Sci.
8
600-618
2007
Sus scrofa (P00371), Sus scrofa, Homo sapiens (P14920), Homo sapiens, Rhodotorula toruloides (P80324), Trigonopsis variabilis (Q99042)
brenda
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
brenda
Sacchi, S.; Bernasconi, M.; Martineau, M.; Mothet, J.P.; Ruzzene, M.; Pilone, M.S.; Pollegioni, L.; Molla, G.
pLG72 modulates intracellular D-serine levels through its interaction with D-amino acid oxidase: Effect on schizophrenia susceptibility
J. Biol. Chem.
283
22244-22256
2008
Homo sapiens, Sus scrofa
brenda
Iwana, S.; Kawazoe, T.; Park, H.K.; Tsuchiya, K.; Ono, K.; Yorita, K.; Sakai, T.; Kusumi, T.; Fukui, K.
Chlorpromazine oligomer is a potentially active substance that inhibits human D-amino acid oxidase, product of a susceptibility gene for schizophrenia
J. Enzyme Inhib. Med. Chem.
23
901-911
2008
Homo sapiens
brenda
Corvin, A.; Donohoe, G.; McGhee, K.; Murphy, K.; Kenny, N.; Schwaiger, S.; Nangle, J.M.; Morris, D.; Gill, M.
D-amino acid oxidase (DAO) genotype and mood symptomatology in schizophrenia
Neurosci. Lett.
426
97-100
2007
Homo sapiens
brenda
Madeira, C.; Freitas, M.E.; Vargas-Lopes, C.; Wolosker, H.; Panizzutti, R.
Increased brain D-amino acid oxidase (DAAO) activity in schizophrenia
Schizophr. Res.
101
76-83
2008
Homo sapiens
brenda
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
brenda
Khoronenkova, S.V.; Tishkov, V.I.
D-amino acid oxidase: physiological role and applications
Biochemistry (Moscow)
73
1511-1518
2008
Homo sapiens, Sus scrofa, Rhodotorula toruloides (P80324), Trigonopsis variabilis (Q99042)
brenda
Hashimoto, K.; Fujita, Y.; Horio, M.; Kunitachi, S.; Iyo, M.; Ferraris, D.; Tsukamoto, T.
Co-administration of a D-amino acid oxidase inhibitor potentiates the efficacy of D-serine in attenuating prepulse inhibition deficits after administration of dizocilpine
Biol. Psychiatry
65
1103-1106
2009
Homo sapiens, Mus musculus
brenda
Nguyen, L.P.; Hsu, E.L.; Chowdhury, G.; Dostalek, M.; Guengerich, F.P.; Bradfield, C.A.
D-amino acid oxidase generates agonists of the aryl hydrocarbon receptor from D-tryptophan
Chem. Res. Toxicol.
22
1897-1904
2009
Homo sapiens, Sus scrofa (P00371)
brenda
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
brenda
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)
brenda
Habl, G.; Zink, M.; Petroianu, G.; Bauer, M.; Schneider-Axmann, T.; von Wilmsdorff, M.; Falkai, P.; Henn, F.A.; Schmitt, A.
Increased D-amino acid oxidase expression in the bilateral hippocampal CA4 of schizophrenic patients: a post-mortem study
J. Neural Transm.
116
1657-1665
2009
Homo sapiens
brenda
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
brenda
Abou El-Magd, R.; Park, H.; Kawazoe, T.; Iwana, S.; Ono, K.; Chung, S.; Miyano, M.; Yorita, K.; Sakai, T.; Fukui, K.
The effect of risperidone on D-amino acid oxidase activity as a hypothesis for a novel mechanism of action in the treatment of schizophrenia
J. Psychopharmacol. (Oxford)
2009
1-13
2009
Homo sapiens, Mus musculus, Sus scrofa
brenda
Verrall, L.; Burnet, P.W.; Betts, J.F.; Harrison, P.J.
The neurobiology of D-amino acid oxidase and its involvement in schizophrenia
Mol. Psychiatry
15
122-137
2009
Homo sapiens
brenda
Wirgenes, K.V.; Djurovic, S.; Agartz, I.; Jonsson, E.G.; Werge, T.; Melle, I.; Andreassen, O.A.
Dysbindin and D-amino-acid-oxidase gene polymorphisms associated with positive and negative symptoms in schizophrenia
Neuropsychobiology
60
31-36
2009
Homo sapiens
brenda
Romano, D.; Molla, G.; Pollegioni, L.; Marinelli, F.
Optimization of human D-amino acid oxidase expression in Escherichia coli
Protein Expr. Purif.
68
72-78
2009
Homo sapiens
brenda
Caldinelli, L.; Molla, G.; Sacchi, S.; Pilone, M.S.; Pollegioni, L.
Relevance of weak flavin binding in human D-amino acid oxidase
Protein Sci.
18
801-810
2009
Homo sapiens
brenda
Mitchell, J.; Paul, P.; Chen, H.J.; Morris, A.; Payling, M.; Falchi, M.; Habgood, J.; Panoutsou, S.; Winkler, S.; Tisato, V.; Hajitou, A.; Smith, B.; Vance, C.; Shaw, C.; Mazarakis, N.D.; de Belleroche, J.
Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase
Proc. Natl. Acad. Sci. USA
107
7556-7561
2010
Homo sapiens
brenda
Caldinelli, L.; Molla, G.; Bracci, L.; Lelli, B.; Pileri, S.; Cappelletti, P.; Sacchi, S.; Pollegioni, L.
Effect of ligand binding on human D-amino acid oxidase: implications for the development of new drugs for schizophrenia treatment
Protein Sci.
19
1500-1512
2010
Homo sapiens (P14920), Homo sapiens
brenda
Sacchi, S.; Caldinelli, L.; Cappelletti, P.; Pollegioni, L.; Molla, G.
Structure-function relationships in human D-amino acid oxidase
Amino Acids
43
1833-1850
2012
Homo sapiens
brenda
Raje, M.; Hin, N.; Duvall, B.; Ferraris, D.V.; Berry, J.F.; Thomas, A.G.; Alt, J.; Rojas, C.; Slusher, B.S.; Tsukamoto, T.
Synthesis of kojic acid derivatives as secondary binding site probes of D-amino acid oxidase
Bioorg. Med. Chem. Lett.
23
3910-3913
2013
Homo sapiens (P14920)
brenda
Hondo, T.; Warizaya, M.; Niimi, T.; Namatame, I.; Yamaguchi, T.; Nakanishi, K.; Hamajima, T.; Harada, K.; Sakashita, H.; Matsumoto, Y.; Orita, M.; Takeuchi, M.
4-Hydroxypyridazin-3(2H)-one derivatives as novel D-amino acid oxidase inhibitors
J. Med. Chem.
56
3582-3592
2013
Homo sapiens
brenda
Pollegioni, L.; Molla, G.
New biotech applications from evolved D-amino acid oxidases
Trends Biotechnol.
29
276-283
2011
Glutamicibacter protophormiae, [Candida] boidinii, Homo sapiens, Rhodotorula toruloides, Trigonopsis variabilis
brenda
Sacchi, S.
D-Serine metabolism new insights into the modulation of D-amino acid oxidase activity
Biochem. Soc. Trans.
41
1551-1556
2013
Homo sapiens
brenda
Hin, N.; Duvall, B.; Berry, J.F.; Ferraris, D.V.; Rais, R.; Alt, J.; Rojas, C.; Slusher, B.S.; Tsukamoto, T.
D-Amino acid oxidase inhibitors based on the 5-hydroxy-1,2,4-triazin-6(1H)-one scaffold
Bioorg. Med. Chem. Lett.
26
2088-2091
2016
Homo sapiens
brenda
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
brenda
Sasabe, J.; Suzuki, M.; Imanishi, N.; Aiso, S.
Activity of D-amino acid oxidase is widespread in the human central nervous system
Front. Synaptic Neurosci.
6
14
2014
Homo sapiens
brenda
Chang, S.L.; Hsieh, C.H.; Chen, Y.J.; Wang, C.M.; Shih, C.S.; Huang, P.W.; Mir, A.; Lane, H.Y.; Tsai, G.E.; Chang, H.T.
The C-terminal region of G72 increases D-amino acid oxidase activity
Int. J. Mol. Sci.
15
29-43
2013
Homo sapiens
brenda
Du, K.; Sun, J.; Song, X.; Song, C.; Feng, W.
Enhancement of the solubility and stability of D-amino acid oxidase by fusion to an elastin like polypeptide
J. Biotechnol.
212
50-55
2015
Homo sapiens
brenda
Hopkins, S.C.; Heffernan, M.L.; Saraswat, L.D.; Bowen, C.A.; Melnick, L.; Hardy, L.W.; Orsini, M.A.; Allen, M.S.; Koch, P.; Spear, K.L.; Foglesong, R.J.; Soukri, M.; Chytil, M.; Fang, Q.K.; Jones, S.W.; Varney, M.A.; Panatier, A.; Oliet, S.H.; Pollegioni, L.; Piubelli, L.; Molla, G.; Nardini, M.; Large, T.H.
Structural, kinetic, and pharmacodynamic mechanisms of D-amino acid oxidase inhibition by small molecules
J. Med. Chem.
56
3710-3724
2013
Homo sapiens (P14920), Homo sapiens
brenda
Hin, N.; Duvall, B.; Ferraris, D.; Alt, J.; Thomas, A.G.; Rais, R.; Rojas, C.; Wu, Y.; Wozniak, K.M.; Slusher, B.S.; Tsukamoto, T.
6-Hydroxy-1,2,4-triazine-3,5(2H,4H)-dione derivatives as novel D-amino acid oxidase inhibitors
J. Med. Chem.
58
7258-7272
2015
Homo sapiens
brenda
Murtas, G.; Caldinelli, L.; Cappelletti, P.; Sacchi, S.; Pollegioni, L.
Human D-amino acid oxidase The inactive G183R variant
Biochim. Biophys. Acta
1866
822-830
2018
Homo sapiens (P14920), Homo sapiens
brenda
Szilagyi, B.; Skok, Z.; Racz, A.; Frlan, R.; Ferenczy, G.G.; Ilas, J.; Keseru, G.M.
Discovery of d-amino acid oxidase inhibitors based on virtual screening against the lid-open enzyme conformation
Bioorg. Med. Chem. Lett.
28
1693-1698
2018
Homo sapiens (P14920)
brenda
Ahn, M.; Park, S.; Jeon, J.; Choi, J.K.; Khang, Y.
Application of an S-layer protein as a self-aggregating tag for cost-effective separation of recombinant human and yeast D-amino acid oxidases in the aqueous two-phase system
Biotechnol. Lett.
42
241-248
2020
Homo sapiens (P14920), Rhodotorula toruloides (P80324), Rhodotorula toruloides ATCC 26217 (P80324)
brenda
Kato, Y.; Hin, N.; Maita, N.; Thomas, A.G.; Kurosawa, S.; Rojas, C.; Yorita, K.; Slusher, B.S.; Fukui, K.; Tsukamoto, T.
Structural basis for potent inhibition of D-amino acid oxidase by thiophene carboxylic acids
Eur. J. Med. Chem.
159
23-34
2018
Homo sapiens (P14920), Homo sapiens
brenda
Rosini, E.; Caldinelli, L.; Piubelli, L.
Assays of D-amino acid oxidase activity
Front. Mol. Biosci.
4
102
2017
Homo sapiens (P14920), Rhodotorula toruloides (P80324)
brenda
Murtas, G.; Sacchi, S.; Valentino, M.; Pollegioni, L.
Biochemical properties of human D-amino acid oxidase
Front. Mol. Biosci.
4
88
2017
Homo sapiens (P14920), Homo sapiens
brenda
Murtas, G.; Sacchi, S.; Pollegioni, L.
Substitution of arginine 120 in human D-amino acid oxidase favors FAD-binding and nuclear mistargeting
Front. Mol. Biosci.
6
125
2019
Homo sapiens (P14920), Homo sapiens
brenda
Jagannath, V.; Brotzakis, Z.; Parrinello, M.; Walitza, S.; Gruenblatt, E.
Controversial effects of D-amino acid oxidase activator (DAOA)/G72 on D-amino acid oxidase (DAO) activity in human neuronal, astrocyte and kidney cell lines The N-methyl D-aspartate (NMDA) receptor hypofunction point of view
Front. Mol. Neurosci.
10
342
2017
Homo sapiens
brenda
Jagannath, V.; Marinova, Z.; Monoranu, C.; Walitza, S.; Gruenblatt, E.
Expression of D-amino acid oxidase (DAO/DAAO) and D-amino acid oxidase activator (DAOA/G72) during development and aging in the human post-mortem brain
Front. Neuroanat.
11
31
2017
Homo sapiens (P14920), Homo sapiens
brenda
Rachadech, W.; Kato, Y.; Abou El-Magd, R.M.; Shishido, Y.; Kim, S.H.; Sogabe, H.; Maita, N.; Yorita, K.; Fukui, K.
P219L substitution in human D-amino acid oxidase impacts the ligand binding and catalytic efficiency
J. Biochem.
168
557-567
2020
Homo sapiens (P14920), Homo sapiens
brenda
Padhi, A.; Hazra, S.
Insights into the role of D-amino acid oxidase mutations in amyotrophic lateral sclerosis
J. Cell. Biochem.
120
2180-2197
2019
Homo sapiens (P14920), Homo sapiens
brenda
Taniguchi, S.; Chosrowjan, H.; Ito, S.; Miyasaka, H.; Katane, M.; Homma, H.; Tanaka, F.; Nueangaudom, A.; Lugsanangarm, K.; Kokpol, S.
Comparative studies on picosecond-resolved fluorescence of D-amino acid oxidases from human with one from porcine kidney. Photoinduced electron transfer from aromatic amino acids to the excited flavin
J. Photochem. Photobiol. B
198
111546
2019
Sus scrofa (P00371), Sus scrofa, Homo sapiens (P14920), Homo sapiens
brenda
Szilagyi, B.; Hargitai, C.; Kelemen, A.A.; Racz, A.; Ferenczy, G.G.; Volk, B.; Keseru, G.M.
Synthesis and biochemical evaluation of lid-open D-amino acid oxidase inhibitors
Molecules
24
290
2019
Homo sapiens (P14920)
brenda
Kohiki, T.; Kato, Y.; Nishikawa, Y.; Yorita, K.; Sagawa, I.; Denda, M.; Inokuma, T.; Shigenaga, A.; Fukui, K.; Otaka, A.
Elucidation of inhibitor-binding pockets of d-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology
Org. Biomol. Chem.
15
5289-5297
2017
Homo sapiens (P14920)
brenda
Kondori, N.; Paul, P.; Robbins, J.; Liu, K.; Hildyard, J.; Wells, D.; De Belleroche, J.
Characterisation of the pathogenic effects of the in vivo expression of an ALS-linked mutation in D-amino acid oxidase Phenotype and loss of spinal cord motor neurons
PLoS ONE
12
e0188912
2017
Homo sapiens (P14920)
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Subramanian, K.; Gora, A.; Spruijt, R.; Mitusinska, K.; Suarez-Diez, M.; Martins Dos Santos, V.; Schaap, P.J.
Modulating D-amino acid oxidase (DAAO) substrate specificity through facilitated solvent access
PLoS ONE
13
e0198990
2018
Sus scrofa (P00371), Sus scrofa, Homo sapiens (P14920), Homo sapiens
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Padhi, A.; Zhang, K.
Mechanistic insights into the loss-of-function mechanisms of rare human D-amino acid oxidase variants implicated in amyotrophic lateral sclerosis
Sci. Rep.
10
17146
2020
Homo sapiens (P14920), Homo sapiens
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Lin, C.H.; Yang, H.T.; Chiu, C.C.; Lane, H.Y.
Blood levels of D-amino acid oxidase vs. D-amino acids in reflecting cognitive aging
Sci. Rep.
7
14849
2017
Homo sapiens (P14920), Homo sapiens
brenda