EC Number   |
Protein Variants |
Reference  |
|---|
    2.3.1.12 | V188A |
ability to be post-translationally lipoylated remains, far-UV CD spectrum differs from wild-type enzyme |
486229 |
| 2.3.1.12 | K136A |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | K153A |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | M131A |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | R135A |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | R135C |
site-directed mutagenesis, additional alkylation of the mutant enzymes with methyl, ethyl, propyl and butyl groups, the modifications cause alterations in interaction of core unit, E1 and E3 in the enzyme complex compared to the wild-type complex, thermodynamics and kinetics in comparison to the wild-type enzyme, overview |
661632 |
| 2.3.1.12 | R135K |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | R135L |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | R135M |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
| 2.3.1.12 | R139A |
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme |
661632 |
