EC Number   |
Protein Variants |
Reference |
|---|
    2.7.2.8 | E17Q |
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine |
692856 |
| 2.7.2.8 | E186A/E387A |
to improve resolution in crystallization |
671144 |
| 2.7.2.8 | E19A |
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 40fold increased compared to wild-type |
722087 |
| 2.7.2.8 | E19R |
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 61fold increased compared to wild-type |
722087 |
| 2.7.2.8 | E19R |
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type |
721268 |
| 2.7.2.8 | E19R |
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation |
738801 |
| 2.7.2.8 | E281A |
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat similar to wild-type, IC50 (L-arginine) 21fold increased compared to wild-type |
722087 |
| 2.7.2.8 | E284D |
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates |
692856 |
| 2.7.2.8 | E416A/K417A |
to improve resolution in crystallization |
671144 |
| 2.7.2.8 | E94A/K95A |
to improve resolution in crystallization |
671144 |
