Cloned (Comment) | Organism |
---|---|
genes F20Hp, C47Ap, and F18Ep, expression of DDO-1, DDO-2, and DDO-3 in Escherichia coli | Caenorhabditis elegans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics in comparison to the human DDO, overview | Caenorhabditis elegans | |
0.68 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
0.8 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
1.06 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans | |
3.81 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
4.2 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
5.54 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans | |
8.87 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
9.23 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
14.6 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | DDO-2 | Caenorhabditis elegans | 5737 | - |
extracellular | DDO-3 | Caenorhabditis elegans | - |
- |
peroxisome | DDO-1 | Caenorhabditis elegans | 5777 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37607 | - |
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation | Caenorhabditis elegans |
37636 | - |
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation | Caenorhabditis elegans |
42501 | - |
x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation | Caenorhabditis elegans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Asp + H2O + O2 | Caenorhabditis elegans | - |
oxaloacetate + NH3 + H2O2 | - |
? | |
D-Glu + H2O + O2 | Caenorhabditis elegans | preferred substrate | 2-oxoglutarate + NH3 + H2O2 | - |
? | |
N-methyl-D-Asp + H2O + O2 | Caenorhabditis elegans | - |
oxaloacetate + methylamine + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Caenorhabditis elegans | - |
gene C47Ap encoding isozyme DDO-1, gene F18Ep encoding isozyme DDO-2, and gene F20Hp encoding isozyme DDO-3 | - |
Purification (Comment) | Organism |
---|---|
recombinant DDO-1, DDO-2, and DDO-3 from Escherichia coli to homogeneity or near homogeneity | Caenorhabditis elegans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Asp + H2O + O2 | - |
Caenorhabditis elegans | oxaloacetate + NH3 + H2O2 | - |
? | |
D-Glu + H2O + O2 | preferred substrate | Caenorhabditis elegans | 2-oxoglutarate + NH3 + H2O2 | - |
? | |
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 | ? | - |
? | |
N-methyl-D-Asp + H2O + O2 | - |
Caenorhabditis elegans | oxaloacetate + methylamine + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation | Caenorhabditis elegans |
Synonyms | Comment | Organism |
---|---|---|
DASPO | - |
Caenorhabditis elegans |
DDO | - |
Caenorhabditis elegans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Caenorhabditis elegans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.76 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
1.52 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
2.51 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
3.01 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
6.04 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
9.49 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
26.1 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans | |
35.4 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans | |
84.5 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.3 | - |
assay at | Caenorhabditis elegans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Caenorhabditis elegans |
General Information | Comment | Organism |
---|---|---|
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 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
172 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
654 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
658 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
1117 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-3 | Caenorhabditis elegans | |
1117 | - |
D-Glu | pH 8.3, 37°C,recombinant DDO-3 | Caenorhabditis elegans | |
2258 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
3759 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-2 | Caenorhabditis elegans | |
3759 | - |
D-Glu | pH 8.3, 37°C,recombinant DDO-2 | Caenorhabditis elegans | |
4712 | - |
D-Asp | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans | |
5787 | - |
N-methyl-D-Asp | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans | |
33440 | - |
D-Glu | pH 8.3, 37°C, recombinant DDO-1 | Caenorhabditis elegans |