EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    1.4.3.16 | more |
the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. No activity with 3-hydroxy-threo-L-aspartate |
Escherichia coli |
? |
- |
? |
| 1.4.3.16 | more |
the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. Catalytic role of the active site residue E121, substrate specificity of wild-type and mutant enzymes, molecular docking studies, role of R290, overview. E121 interacts favourably with the charged amino group of the substrate and different ligands might assume different orientations in the active site of the enzyme, binding modes for L-aspartate, overview |
Escherichia coli |
? |
- |
? |
| 1.4.3.16 | more |
the enzyme does not show activity on L-phenylalanine (50100 mM), L-glutamate (50100 mM), glycine (50100 mM), L-proline (50100 mM) and L-alanine (50100 mM) |
Sulfurisphaera tokodaii |
? |
- |
? |
| 1.4.3.16 | more |
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine |
Sulfurisphaera tokodaii |
? |
- |
? |
| 1.4.3.16 | N-acetyl-L-aspartate + O2 |
- |
Escherichia coli |
? + H2O2 |
- |
? |
| 1.4.3.16 | N-formyl-L-aspartate + O2 |
- |
Escherichia coli |
? + H2O2 |
- |
? |
