EC Number   |
Protein Variants |
Reference |
|---|
    4.3.3.7 | A204R |
site-directed mutagenesis, disruption of the native tetramer formation by targeting the dimer-dimer interface. The mutant enzyme is a dimeric protein with an identical fold and active-site structure to the tetrameric wild-type enzyme |
713969 |
| 4.3.3.7 | A49K |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
729062 |
| 4.3.3.7 | A49P |
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme and is still sensitive to L-lysine |
-, 729062 |
| 4.3.3.7 | A49W |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
729062 |
| 4.3.3.7 | C139A |
site-directed in silico mutation |
729694 |
| 4.3.3.7 | D193A |
removal of water mediated hydrogen-bond network |
701934 |
| 4.3.3.7 | D193Y |
removal of water mediated hydrogen-bond network and introduction of steric bulk to alter surface topology |
701934 |
| 4.3.3.7 | E84T |
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme and is insensitive to L-lysine |
-, 729062 |
| 4.3.3.7 | H118Y |
mutant enzyme H56K is more conducive to L-lysine production than mutant H118Y |
-, 747010 |
| 4.3.3.7 | H56K |
mutant enzyme H56K is more conducive to L-lysine production than mutant H118Y |
-, 747010 |
