EC Number   |
Protein Variants |
Reference |
|---|
    5.3.3.1 | D103A |
site-directed mutagenesis of the catalytic residue, the mutant shows 5000fold reduced activity compared tot he wild-type enzyme |
682479 |
| 5.3.3.1 | D103N/D40N |
site-directed mutagenesis, 3,4,5-trifluorophenol bind as ionized phenolate to KSI containing the D103N mutation |
702327 |
| 5.3.3.1 | D241N |
mutant enzyme nearly has full isomerase activity, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity. Mutant enzyme has a basal isomerase activity in the absence of coenzyme that is 10% of the NADH-stimulated turnover number |
652452 |
| 5.3.3.1 | D257L |
complete lack of isomerase activity in absence of coenzyme, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity |
652452 |
| 5.3.3.1 | D258L |
complete lack of isomerase activity in absence of coenzyme, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity |
652452 |
| 5.3.3.1 | D265N |
complete lack of isomerase activity in absence of coenzyme, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity |
652452 |
| 5.3.3.1 | D36A/K37R |
mutation shifts the cofactor preference of both 3-beta-hydroxysteroid dehydrogenase and isomerase from NAD(H) to NADP(H) |
652452 |
| 5.3.3.1 | D38A |
the catalytic turnover number is 140fold less than that for the wild-type |
649966 |
| 5.3.3.1 | D38A/D99N |
no detectable activity |
649966 |
| 5.3.3.1 | D38A/Y14F |
no detectable activity |
649966 |
