EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.4.3.25 | L-arginine + H2O + O2 |
- |
Synechococcus elongatus PCC 7942 = FACHB-805 |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Synechococcus elongatus |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Synechococcus cedorum |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Oceanobacter kriegii |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Pseudomonas sp. |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
the enzyme catalyzes the oxidative deamination of L-arginine and converts L-arginine to 2-ketoarginine, which is nonenzymatically converted into 4-guanidinobutyric acid when the hydrogen peroxide formed by L-arginine oxidation is not removed |
? |
1.4.3.25 | L-arginine + H2O + O2 |
wild-type L-glutamate oxidase enzyme shows strict substrate specificity for L-glutamate. The R305E mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine |
Streptomyces sp. X-119-6 |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Pseudomonas sp. TPU 7192 |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
the enzyme catalyzes the oxidative deamination of L-arginine and converts L-arginine to 2-ketoarginine, which is nonenzymatically converted into 4-guanidinobutyric acid when the hydrogen peroxide formed by L-arginine oxidation is not removed |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Synechococcus cedorum PCC 6908 |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-arginine + H2O + O2 |
- |
Synechococcus elongatus PCC 7942 |
5-guanidino-2-oxopentanoate + NH3 + H2O2 |
- |
? |
1.4.3.25 | L-canavanine + H2O + O2 |
- |
Pseudomonas sp. |
2-oxocanavanine + NH3 + H2O2 |
- |
? |