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Literature summary extracted from
- Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases (2007), FEBS J., 274, 137-149.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.3.1 | the C47A10.5 gene product is expressed in Escherichia coli as recombinant protein with an N-terminal His-tag | Caenorhabditis elegans |
| 1.4.3.1 | the F18E3.7a gene product is expressed in Escherichia coli as recombinant protein with an N-terminal His-tag | Caenorhabditis elegans |
| 1.4.3.1 | the His-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells | Caenorhabditis elegans |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.3.1 | 0.23 | - |
D-glutamate | 37°C, pH 8.3, C47A10.5 gene product | Caenorhabditis elegans |  |
| 1.4.3.1 | 0.23 | - |
D-glutamate | recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 0.25 | - |
D-glutamate | 37°C, pH 8.3, F18E3.7a gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 0.25 | - |
D-glutamate | recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 0.38 | - |
D-Aspartate | 37°C, pH 8.3, F18E3.7a gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 0.38 | - |
D-asparagine | recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 0.84 | - |
N-Methyl-D-aspartate | 37°C, pH 8.3, C47A10.5 gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 0.84 | - |
N-methyl-D-asparagine | recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 1.84 | - |
N-Methyl-D-aspartate | 37°C, pH 8.3, F18E3.7a gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 1.84 | - |
N-methyl-D-asparagine | recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 2.02 | - |
D-Aspartate | 37°C, pH 8.3, C47A10.5 gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 2.02 | - |
D-asparagine | recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.4.3.1 | 37610 | - |
F18Ep, calculated from sequence of cDNA | Caenorhabditis elegans |
| 1.4.3.1 | 37640 | - |
C47Ap, calculated from sequence of cDNA | Caenorhabditis elegans |
| 1.4.3.1 | 41770 | - |
His-tagged F18Ep, calculated from sequence of cDNA | Caenorhabditis elegans |
| 1.4.3.1 | 41790 | - |
His-tagged C47Ap, calculated from sequence of cDNA | Caenorhabditis elegans |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.3.1 | Caenorhabditis elegans | - |
- |
- |
| 1.4.3.1 | Caenorhabditis elegans | - |
at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.4.3.1 | HiTrap Chelating HP column chromatography | Caenorhabditis elegans |
| 1.4.3.1 | recombinant C47A10.5 gene product | Caenorhabditis elegans |
| 1.4.3.1 | recombinant F18E3.7a gene product | Caenorhabditis elegans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.3.1 | D-alanine + H2O + O2 | C47Ap exhibits 4.5% activity and F18Ep exhibits 2.8% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | D-arginine + H2O + O2 | C47Ap exhibit less than 0.1% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | D-asparagine + H2O + O2 | C47Ap exhibits 17% activity and F18Ep exhibits 6.1% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | D-aspartate + H2O + O2 | 100% activity | Caenorhabditis elegans | oxaloacetate + NH3 + H2O2 | - |
? | |
| 1.4.3.1 | D-aspartate + H2O + O2 | at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization | Caenorhabditis elegans | oxaloacetate + NH3 + H2O2 | - |
? | |
| 1.4.3.1 | D-glutamate + H2O + O2 | activity is 2.5fold higher than with D-Asp, F18E3.7a gene product | Caenorhabditis elegans | 2-oxoglutarate + NH3 + H2O2 | - |
? | |
| 1.4.3.1 | D-glutamate + H2O + O2 | activity is 67% of the activity with D-Asp, C47A10.5 gene product | Caenorhabditis elegans | 2-oxoglutarate + NH3 + H2O2 | - |
? | |
| 1.4.3.1 | D-glutamate + H2O + O2 | at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization | Caenorhabditis elegans | 2-oxoglutarate + NH3 + H2O2 | - |
? | |
| 1.4.3.1 | D-glutamate + H2O + O2 | C47Ap exhibits 247% activity and F18Ep exhibits 67% activity compared to D-aspartate as substrate | Caenorhabditis elegans | 2-oxoglutarate + NH3 + H2O2 | - |
? | |
| 1.4.3.1 | D-methionine + H2O + O2 | C47Ap exhibits 3.8% activity and F18Ep exhibits 2.4% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | L-asparagine + H2O + O2 | C47Ap exhibits 2.6% activity and F18Ep exhibits less than 0.1% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | L-glutamine + H2O + O2 | C47Ap exhibits 1.3% activity and F18Ep exhibits 0.3% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | additional information | no detectable activity with L-alanine, L-methionine, and L-arginine | Caenorhabditis elegans | ? | - |
? | |
| 1.4.3.1 | N-methyl-D-asparagine + H2O + O2 | - |
Caenorhabditis elegans | ? | - |
r | |
| 1.4.3.1 | N-methyl-D-aspartate + H2O + O2 | activity is 1.1fold higher than with D-Asp, C47A10.5 gene product | Caenorhabditis elegans | oxaloacetate + CH3NH2 + H2O2 | - |
? | |
| 1.4.3.1 | N-methyl-D-aspartate + H2O + O2 | activity is 3.1fold higher than with D-Asp, F18E3.7a gene product | Caenorhabditis elegans | oxaloacetate + CH3NH2 + H2O2 | - |
? | |
| 1.4.3.1 | N-methyl-D-aspartate + H2O + O2 | C47Ap exhibits 313% activity and F18Ep exhibits 110% activity compared to D-aspartate as substrate | Caenorhabditis elegans | oxaloacetate + CH3NH2 + H2O2 | - |
? | |
| 1.4.3.1 | N-methyl-L-asparagine + H2O + O2 | C47Ap exhibits 6.7% activity and F18Ep exhibits 1.1% activity compared to D-aspartate as substrate | Caenorhabditis elegans | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.3.1 | C47A10.5 gene product | - |
Caenorhabditis elegans |
| 1.4.3.1 | C47Ap | - |
Caenorhabditis elegans |
| 1.4.3.1 | C47Ap | the protein with DASPO activity shows distinct kinetic properties against D-Asp, D-Glu, and N-methyl-D-Asp | Caenorhabditis elegans |
| 1.4.3.1 | DASPO | - |
Caenorhabditis elegans |
| 1.4.3.1 | F18E3.7a gene product | - |
Caenorhabditis elegans |
| 1.4.3.1 | F18Ep | - |
Caenorhabditis elegans |
| 1.4.3.1 | F18Ep | the protein with DASPO activity shows distinct kinetic properties against D-Asp, D-Glu, and N-methyl-D-Asp | 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 | 2.11 | - |
D-glutamate | 37°C, pH 8.3, F18E3.7a gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 2.11 | - |
D-glutamate | recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 3 | - |
N-Methyl-D-aspartate | 37°C, pH 8.3, F18E3.7a gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 3 | - |
N-methyl-D-asparagine | recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 3.07 | - |
D-Aspartate | 37°C, pH 8.3, F18E3.7a gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 3.07 | - |
D-asparagine | recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 3.13 | - |
D-Aspartate | 37°C, pH 8.3, C47A10.5 gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 4.29 | - |
D-asparagine | recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 5.31 | - |
D-glutamate | 37°C, pH 8.3, C47A10.5 gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 5.31 | - |
D-glutamate | recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
| 1.4.3.1 | 6.13 | - |
N-Methyl-D-aspartate | 37°C, pH 8.3, C47A10.5 gene product | Caenorhabditis elegans | |
| 1.4.3.1 | 6.13 | - |
N-methyl-D-asparagine | recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C | Caenorhabditis elegans | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.3.1 | FAD | - |
Caenorhabditis elegans | |
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