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Literature summary extracted from

  • Katane, M.; Saitoh, Y.; Seida, Y.; Sekine, M.; Furuchi, T.; Homma, H.
    Comparative characterization of three D-aspartate oxidases and one D-amino acid oxidase from Caenorhabditis elegans (2010), Chem. Biodivers., 7, 1424-1434.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.1 genes F20Hp, C47Ap, and F18Ep, expression of DDO-1, DDO-2, and DDO-3 in Escherichia coli Caenorhabditis elegans
1.4.3.3 gene Y69Ap, expression of DAO in Escherichia coli Caenorhabditis elegans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.1 additional information
-
 additional information kinetics in comparison to the human DDO, overview Caenorhabditis elegans
1.4.3.1 0.68
-
 D-Glu pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 0.8
-
 D-Glu pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 1.06
-
 D-Glu pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.1 3.81
-
 D-Asp pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 4.2
-
 D-Asp pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 5.54
-
 D-Asp pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.1 8.87
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 9.23
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 14.6
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.3 additional information
-
 additional information kinetics in comparison to the human enzyme, overview Caenorhabditis elegans
1.4.3.3 1.01
-
 D-Arg pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 2.72
-
 D-Phe pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 2.89
-
 D-His pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 6.89
-
 D-Ala pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 20
-
 D-Ser pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.3.1 cytoplasm DDO-2 Caenorhabditis elegans 5737
-
1.4.3.1 extracellular DDO-3 Caenorhabditis elegans
-
-
1.4.3.1 peroxisome DDO-1 Caenorhabditis elegans 5777
-
1.4.3.3 peroxisome
-
 Caenorhabditis elegans 5777
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.1 37607
-
 x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation Caenorhabditis elegans
1.4.3.1 37636
-
 x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation Caenorhabditis elegans
1.4.3.1 42501
-
 x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation Caenorhabditis elegans
1.4.3.3 36117
-
 x * 36117, sequence calculation Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.1 D-Asp + H2O + O2 Caenorhabditis elegans
-
 oxaloacetate + NH3 + H2O2
-
 ?
1.4.3.1 D-Glu + H2O + O2 Caenorhabditis elegans preferred substrate 2-oxoglutarate + NH3 + H2O2
-
 ?
1.4.3.1 N-methyl-D-Asp + H2O + O2 Caenorhabditis elegans
-
 oxaloacetate + methylamine + H2O2
-
 ?
1.4.3.3 D-Ala + H2O + O2 Caenorhabditis elegans
-
 pyruvate + NH3 + H2O2
-
 ?
1.4.3.3 D-Arg + H2O + O2 Caenorhabditis elegans
-
 5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
 ?
1.4.3.3 D-His + H2O + O2 Caenorhabditis elegans
-
 3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
 ?
1.4.3.3 D-Phe + H2O + O2 Caenorhabditis elegans
-
 phenylpyruvate + NH3 + H2O2
-
 ?
1.4.3.3 D-Ser + H2O + O2 Caenorhabditis elegans
-
 2-oxo-3-hydroxypropionate + NH3 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.1 Caenorhabditis elegans
-
 gene C47Ap encoding isozyme DDO-1, gene F18Ep encoding isozyme DDO-2, and gene F20Hp encoding isozyme DDO-3
-
1.4.3.3 Caenorhabditis elegans
-
 gene Y69Ap
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.1 recombinant DDO-1, DDO-2, and DDO-3 from Escherichia coli to homogeneity or near homogeneity Caenorhabditis elegans
1.4.3.3 recombinant DAO from Escherichia coli to homogeneity Caenorhabditis elegans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.1 D-Asp + H2O + O2
-
 Caenorhabditis elegans oxaloacetate + NH3 + H2O2
-
 ?
1.4.3.1 D-Glu + H2O + O2 preferred substrate Caenorhabditis elegans 2-oxoglutarate + NH3 + H2O2
-
 ?
1.4.3.1 additional information all Caenorhabditis elegans DDOs exhibit the highest catalytic efficiency for D-Glu, but their efficiencies differ considerably for D-Glu, D-Asp, and NMDA. The isozymes show only very low or undetectable levels of activity against the neutral and basic D-amino acids and no activity with L-amino acids and N-methyl-L-Asp Caenorhabditis elegans ?
-
 ?
1.4.3.1 N-methyl-D-Asp + H2O + O2
-
 Caenorhabditis elegans oxaloacetate + methylamine + H2O2
-
 ?
1.4.3.3 D-Ala + H2O + O2
-
 Caenorhabditis elegans pyruvate + NH3 + H2O2
-
 ?
1.4.3.3 D-Arg + H2O + O2
-
 Caenorhabditis elegans 5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
 ?
1.4.3.3 D-His + H2O + O2
-
 Caenorhabditis elegans 3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
 ?
1.4.3.3 D-Phe + H2O + O2
-
 Caenorhabditis elegans phenylpyruvate + NH3 + H2O2
-
 ?
1.4.3.3 D-Ser + H2O + O2
-
 Caenorhabditis elegans 2-oxo-3-hydroxypropionate + NH3 + H2O2
-
 ?
1.4.3.3 additional information DAO shows no activity with D-Asp, N-methyl-D-Asp, and D-Glu Caenorhabditis elegans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.1 ? x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation Caenorhabditis elegans
1.4.3.3 ? x * 36117, sequence calculation Caenorhabditis elegans

Synonyms

EC Number Synonyms Comment Organism
1.4.3.1 DASPO
-
 Caenorhabditis elegans
1.4.3.1 DDO
-
 Caenorhabditis elegans
1.4.3.3 DAAO
-
 Caenorhabditis elegans
1.4.3.3 DAO
-
 Caenorhabditis elegans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.1 37
-
 assay at Caenorhabditis elegans
1.4.3.3 37
-
 assay at Caenorhabditis elegans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.1 0.76
-
 D-Glu pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 1.52
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 2.51
-
 D-Asp pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 3.01
-
 D-Glu pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 6.04
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 9.49
-
 D-Asp pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 26.1
-
 D-Asp pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.1 35.4
-
 D-Glu pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.1 84.5
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.3 1.51
-
 D-Ser pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 1.51
-
 D-His pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 2.83
-
 D-Arg pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 14.9
-
 D-Ala pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 25.1
-
 D-Phe pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.1 8.3
-
 assay at Caenorhabditis elegans
1.4.3.3 8.3
-
 assay at Caenorhabditis elegans

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.1 FAD
-
 Caenorhabditis elegans
1.4.3.3 FAD
-
 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
1.4.3.1 physiological function D-Asp oxidase is a FAD-containing flavoprotein that catalyzes the oxidative deamination of D-amino acids with O2 to generate the corresponding 2-oxo acids, along with H2O2 and NH3. DDO is highly specific for acidic D-amino acids, such as D-Asp, N-methyl-D-Asp, and D-Glu Caenorhabditis elegans
1.4.3.3 physiological function D-amino acid oxidase is a FAD-containing flavoprotein that catalyzes the oxidative deamination of D-amino acids with O2 to generate the corresponding 2-oxo acids, along with H2O2 and NH3 Caenorhabditis elegans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.4.3.1 172
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 654
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 658
-
 D-Asp pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 1117
-
 D-Glu pH 8.3, 37°C, recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 1117
-
 D-Glu pH 8.3, 37°C,recombinant DDO-3 Caenorhabditis elegans
1.4.3.1 2258
-
 D-Asp pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 3759
-
 D-Glu pH 8.3, 37°C, recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 3759
-
 D-Glu pH 8.3, 37°C,recombinant DDO-2 Caenorhabditis elegans
1.4.3.1 4712
-
 D-Asp pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.1 5787
-
 N-methyl-D-Asp pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.1 33440
-
 D-Glu pH 8.3, 37°C, recombinant DDO-1 Caenorhabditis elegans
1.4.3.3 75
-
 D-Ser pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 521
-
 D-His pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 2165
-
 D-Ala pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 2802
-
 D-Arg pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans
1.4.3.3 9215
-
 D-Phe pH 8.3, 37°C, recombinant DAO Caenorhabditis elegans