Protein Variants | Comment | Organism |
---|---|---|
T70F | nearly no activity with L-erythro-3-hydroxyaspartate, in opposite to the wild-type, altered reaction kinetics due to inability to stabilize the reaction quinonoid intermediate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Escherichia coli | |
additional information | - |
additional information | wild-type and mutants | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + 2-oxoglutarate | Escherichia coli | - |
oxaloacetate + L-glutamate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate | mechanism | Escherichia coli | |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate | intermediate formation | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? | |
L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
r | |
L-erythro-3-hydroxyaspartate + 2-oxoglutarate | high stabilization of the quinonoid intermediate formed by L-erythro-3-hydroxyaspartate and pyridoxal 5'-phosphate at the active site via Tyr70, kinetic analysis | Escherichia coli | erythro-3-hydroxy-2-oxoaspartate + L-glutamate | - |
? | |
L-erythro-3-hydroxyaspartate + 2-oxoglutarate | wild-type, no activity with mutant T70F | Escherichia coli | erythro-3-hydroxy-2-oxoaspartate + L-glutamate | - |
? |