EC Number |
Protein Variants |
Reference |
---|
1.1.1.357 | F217S |
mutation converts AKR1C33 into a dually coenzyme-specific form and abolishes the activity towards 3-keto-5beta-cholestanes that are substrates specific to AKR1C33, and markedly decreases the sensitivity to 4-pregnenes |
739957 |
1.1.1.357 | H216F |
the mutation decreases 3fold the Km for NADP+. The kinetic constants for bile acids with a 12alpha-hydroxy group are decreased 1.5-7fold and those for the other substrates are increased 1.3-9fold. The mutation decreases the stimulatory effects of the enzyme activity by sulfobromophthalein, clofibric acid and thyroxine, which increases the Km for the coenzyme and substrate of the mutant enzymes more highly than those of the wild type enzyme |
724209 |
1.1.1.357 | H216L |
inactive |
724209 |
1.1.1.357 | H216W |
inactive |
724209 |
1.1.1.357 | H216Y |
the mutation decreases 3fold the Km for NADP+. The kinetic constants for bile acids with a 12alpha-hydroxy group are decreased 1.5-7fold and those for the other substrates are increased 1.3-9fold. The mutation decreases the stimulatory effects of the enzyme activity by sulfobromophthalein, clofibric acid and thyroxine, which increases the Km for the coenzyme and substrate of the mutant enzymes more highly than those of the wild type enzyme |
724209 |
1.1.1.357 | K157A |
site-directed mutagenesis of a catalytic site residue, the NADH binding affinity of K157A mutant is much lower than that of the wild-type resulting in a decreased kcat |
760734 |
1.1.1.357 | more |
when a specific siRNA is used to suppress 3alpha-HSD3 expression without interfering with 3alpha-HSD4, which shares a highly homologous active site, the 5alpha-DHT concentration increases, whereas MCF-7 cell growth is suppressed. Downregulation of 3alpha-HSD3 decreases MCF-7 breast cancer cell growth |
740017 |
1.1.1.357 | N272T |
mutation does not influence cofactor specificity |
739957 |
1.1.1.357 | P185A |
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme |
743632 |
1.1.1.357 | P185G |
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme |
743632 |