EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.62 | A170E/F172E |
no detectable activity |
287194 |
| 1.1.1.62 | A50R |
site-directed mutagenesis, the mutant shows increased rates of NADPH dissociation and thus enhanced substrate oxidation with NADP+ compared to the wild-type enzyme |
675979 |
| 1.1.1.62 | C10S |
site-directed mutagenesis, substitution of Cys10 with Ser results in a decreased protein half-life, without significantly altering kinetic properties. Mutant Cys10Ser shows approximately 50% lower activity compared to the wild-type. Mutating Cys10 to Ser does not lead to significant changes in contacts between Ser10 and Ile7, Gly9 and Ala34. But all three contacts between Ser10 and Gly15 are shorter than between Cys10 and Gly15, and Gly15 is more distant from a phosphate oxygen on NADP+ |
740542 |
| 1.1.1.62 | C10S |
site-directed mutagenesis, the Cys10Ser mutant 17beta-HSD1 is partially protected from inhibition by NEM and dithiocarbamates. Mutating Cys10 to Ser does not lead to significant changes in contacts between Ser10 and Ile7, Gly9 and Ala34, but all three contacts between Ser10 and Gly15 are shorter than between Cys10 and Gly15, and Gly15 is more distant from a phosphate oxygen on NADP+ |
740542 |
| 1.1.1.62 | H111A |
site-directed mutagenesis, the mutant is dimeric like the wild-type enzyme, inactive mutant |
672789 |
| 1.1.1.62 | H111L |
site-directed mutagenesis, the mutation renders the enzyme monomeric, inactive mutant |
672789 |
| 1.1.1.62 | H164G |
mutation results in a conformation of the enzyme that possesses a higher catalytic activity |
687869 |
| 1.1.1.62 | H164W |
mutation results in a conformation of the enzyme that possesses a higher catalytic activity |
687869 |
| 1.1.1.62 | H210A/H213A |
decreased activity |
287207 |
| 1.1.1.62 | H221A |
catalytic efficiency is reduced 20fold for oxidative reaction and 11fold for the reductive reaction |
287207 |
