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Literature summary for 1.4.3.25 extracted from
- Following the evolutionary track of a highly specific L-arginine oxidase by reconstruction and biochemical analysis of ancestral and native enzymes (2019), Appl. Environ. Microbiol., 85, e00459-19 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oceanobacter kriegii | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginine + H2O + O2 | - |
Oceanobacter kriegii | 5-guanidino-2-oxopentanoate + NH3 + H2O2 | - |
? |  |
| L-lysine + H2O + O2 | 15% of the activity with L-arginine | Oceanobacter kriegii | 2-oxolysine + NH3 + H2O2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aroD | - |
Oceanobacter kriegii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | FAD-dependent enzyme | Oceanobacter kriegii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | L-arginine oxidase evolves from a highly thermostable and promiscuous FAD-dependent amino acid oxidase | Oceanobacter kriegii |
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Release 2023.1 (January 2023)
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