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Literature summary for 1.4.3.16 extracted from
- L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase (1982), J. Biol. Chem., 257, 626-632.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| L-aspartate | substrate activation above 1.0 mM | Escherichia coli |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | competitive to FAD | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + H2O + O2 | Escherichia coli | first enzyme of quinolinate synthetase system | oxaloacetate + NH3 + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + H2O + O2 | - |
Escherichia coli | oxaloacetate + NH3 + H2O2 | - |
? | |
| L-aspartate + H2O + O2 | first enzyme of quinolinate synthetase system | Escherichia coli | oxaloacetate + NH3 + H2O2 | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | flavoprotein | Escherichia coli | |
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