Crystallization (Comment) | Organism |
---|---|
crystals are grown at 19°C by the hanging-drop technique, unliganded and hydrocinnamate complex of V39L/K41Y/T47I/N69L/T109S/A293D/N297S, hydrocinnamate complex and maleate complexes of A12T/P13T/N34D/T109S/G261A/S285G/N297S and the hydrocinnamate complex of A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | mutant enzyme has nearly the same ratio of kcat/Km(Phe) to kcat/Km(Asp) as that of wild-type enzyme. The additional mutation A293D compared to mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/N297S holds the Arg292 side chain away from the active site to allow increased specificity for phenylalanine over aspartate | Escherichia coli |
V39L/K41Y/T47I/N69L/T109S/A293D/N297S | the additional mutation A293D compared to mutant enzyme V39L/K41Y/T47I/N69L/T109S/N297S holds the Arg292 side chain away from the active site to allow increased specificity for phenylalanine over aspartate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
L-Phe | pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli | |
0.48 | - |
2-oxoglutarate | pH 8, cosubstrate: L-Phe, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli | |
2.6 | - |
2-oxoglutarate | pH 8, cosubstrate: L-Asp, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli | |
29 | - |
L-Asp | pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P00509 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? | |
L-Phe + 2-oxoglutarate | - |
Escherichia coli | 2-oxo-3-phenylpropionic acid + L-glutamate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
10 | - |
L-Phe | pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli | |
43 | - |
L-Asp | pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S | Escherichia coli |