EC Number   |
Protein Variants |
Reference |
|---|
    2.6.1.1 | 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 |
658035 |
| 2.6.1.1 | A168G |
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type |
759965 |
| 2.6.1.1 | C166A |
site-directed mutagenesis of isozyme mAspAT, decreased ability to undergo transition from the open to the closed conformation essential for the reaction mechanism, reduced reactivity with DTNB |
639875 |
| 2.6.1.1 | C166S |
site-directed mutagenesis of isozyme mAspAT, decreased ability to undergo transition from the open to the closed conformation essential for the reaction mechanism, reduced reactivity with DTNB |
639875 |
| 2.6.1.1 | D220A |
mutation in pyridoxal phosphate-binding residue, almost complete loss of activity |
739452 |
| 2.6.1.1 | D232N |
mutant shows no activity |
722235 |
| 2.6.1.1 | DELTA1-13 |
truncation of these noncatalytic residues reduces enzyme activity and a peptide containing these amino acids inhibits PfAspAT in vitro and in the lysate of cultured parasites |
722976 |
| 2.6.1.1 | DELTA1-7 |
truncation of the first seven amino acids only minorly reduces enzymatic activity |
722976 |
| 2.6.1.1 | E108K |
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type |
759965 |
| 2.6.1.1 | E265K |
site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate |
639884 |
