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Literature summary for 1.4.3.3 extracted from

  • Murtas, G.; Sacchi, S.; Valentino, M.; Pollegioni, L.
    Biochemical properties of human D-amino acid oxidase (2017), Front. Mol. Biosci., 4, 88 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
6-chlorobenzo[d]isoxazol-3-ol a decrease in protein fluorescence is observed at increasing 6-chlorobenzo[d]isoxazol-3-ol concentrations Homo sapiens
benzoate a decrease in protein fluorescence is observed at increasing concentrations, with a biphasic change Homo sapiens
D-Dopa
-
Homo sapiens
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) Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
D-cysteine pH 8.5, 25°C Homo sapiens
0.7
-
D-kynurenine pH 8.5, 25°C Homo sapiens
6
-
D-Dopa pH 8.5, 25°C Homo sapiens
83.5
-
D-cycloserine pH 8.5, 25°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information divalent ions and nucleotides do not affect enzyme function Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P14920
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-alanine + H2O + O2
-
Homo sapiens pyruvate + H2O2 + NH3
-
?
D-aspartate + H2O + O2
-
Homo sapiens oxaloacetate + NH3 + H2O2
-
?
D-cycloserine + H2O + O2
-
Homo sapiens ? + NH3 + H2O2
-
?
D-cysteine + H2O + O2
-
Homo sapiens 2-oxo-3-sulfanylpropionate + NH3 + H2O2
-
?
D-DOPA + H2O + O2
-
Homo sapiens 3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
?
D-glutamate + H2O + O2
-
Homo sapiens 2-oxoglutarate + NH3 + H2O2
-
?
D-kynurenine + H2O + O2
-
Homo sapiens kynurenate + NH3 + H2O2
-
?
D-phenylalanine + H2O + O2
-
Homo sapiens phenylpyruvate + NH3 + H2O2
-
?
D-proline + H2O + O2
-
Homo sapiens 2-oxopentanoate + NH3 + H2O2
-
?
D-serine + H2O + O2
-
Homo sapiens 2-oxo-3-hydroxypropanoate + NH3 + H2O2
-
?
D-tyrosine + H2O + O2
-
Homo sapiens 3-(4-hydroxyphenyl)pyruvate + NH3 + H2O2
-
?
glycine + H2O + O2
-
Homo sapiens glyoxylate + NH3 + H2O2
-
?
additional information DAAO is mainly active on neutral, hydrophobic and slightly polar D-amino acids and shows a preference for aromatic amino acids Homo sapiens ?
-
-
N-methyl-D-aspartate + H2O + O2
-
Homo sapiens oxaloacetate + methylamine + H2O2
-
?
tryptophan + H2O + O2
-
Homo sapiens indol-3-pyruvic acid + NH3 + H2O2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
60 min pH 8.5, fully stable Homo sapiens
65
-
60 min, complete inactivation Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.09
-
D-kynurenine pH 8.5, 25°C Homo sapiens
0.77
-
D-cycloserine pH 8.5, 25°C Homo sapiens
8.6
-
D-cysteine pH 8.5, 25°C Homo sapiens
40.5
-
D-Dopa pH 8.5, 25°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
substrate D-serine Homo sapiens
10
-
substrate D-alanine Homo sapiens

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 10 60 min, fully stable within Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD Kd value 0.008 mM for FAD-apoprotein complex. Benzoate binding favors a protein conformation with a higher affinity for the cofactor FAD Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
41.3
-
D-Dopa pH 8.5, 25°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.009
-
D-cycloserine pH 8.5, 25°C Homo sapiens
0.14
-
D-kynurenine pH 8.5, 25°C Homo sapiens
6.75
-
D-Dopa pH 8.5, 25°C Homo sapiens
14.6
-
D-cysteine pH 8.5, 25°C Homo sapiens