EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.169 | A181L |
site-directed mutagenesis, the substitution displaces Ser239 and increases the Km for ketopantoate 844fold, without affecting kcat. The decrease in 2-dehydropantoate affinity enhances the already kinetically preferred NADPH binding path, making the random mechanism appear to be sequentially ordered and reducing the kinetic cooperativity |
740065 |
| 1.1.1.169 | A181L |
the substitution increases the Km of ketopantoate 844fold, without affecting the kcat value |
740065 |
| 1.1.1.169 | C84A |
site-directed mutagenesis |
-, 739822 |
| 1.1.1.169 | C84A |
site-directed mutagenesis, crystal structure analysis, overview |
-, 741385 |
| 1.1.1.169 | D248A |
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain |
667687 |
| 1.1.1.169 | D248A |
site-directed mutagenesis, wild-type activity |
286109 |
| 1.1.1.169 | E210A |
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain |
667687 |
| 1.1.1.169 | E210A |
site-directed mutagenesis, wild-type activity |
286109 |
| 1.1.1.169 | E240A |
site-directed mutagenesis, wild-type activity |
286109 |
| 1.1.1.169 | E256A |
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview |
687675 |
