EC Number   |
Protein Variants |
Reference |
|---|
    2.7.2.8 | A26V |
site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme |
738801 |
| 2.7.2.8 | D162E |
about 0.1% of wild-type activity |
659704 |
| 2.7.2.8 | DELTA2-15 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 71fold increased compared to wild-type |
722087 |
| 2.7.2.8 | DELTA2-19 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 148fold increased compared to wild-type |
722087 |
| 2.7.2.8 | DELTA2-29 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 163fold increased compared to wild-type |
722087 |
| 2.7.2.8 | DELTA25 |
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 17fold increased compared to wild-type |
722087 |
| 2.7.2.8 | DELTA357-513 |
truncated mutant lacking C-terminal 150 amino acids (spanning residues 38-356), belonging to the DUF619 domain family, shows that is it stabilizes yNAGK, slows catalysis and modulates feed-back inhibition by arginine. Truncated yNAGK shows doubled kcat compared to wild-type, Km is almost not affected. IC50 (L-arginine) is lowered compared to wild-type. Truncated mutand shows lower thermal stability compared to wild-type |
723557 |
| 2.7.2.8 | DELTA8 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 16fold increased compared to wild-type |
722087 |
| 2.7.2.8 | E17A |
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine |
692856 |
| 2.7.2.8 | E17D |
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine |
692856 |
