EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.50 | more |
construction of insertion mutants, overview |
687870 |
| 1.1.1.50 | Y155F |
decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants |
711310 |
| 1.1.1.50 | K159A |
decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by residues K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis. Residue N86 is important for stabilizing the position of K159 |
711310 |
| 1.1.1.50 | N86A |
decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by residues K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis. Residue N86 is important for stabilizing the position of K159 |
711310 |
| 1.1.1.50 | Y155F |
decrease in the catalytic constant by 220fold and increase in the dissociation constant by 3fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis |
711310 |
| 1.1.1.50 | N86A |
decrease in the catalytic constant by 37fold and increase in the dissociation constant by 8fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Residue N86 is important for stabilizing the position of K159 |
711310 |
| 1.1.1.50 | K159A |
decrease in the catalytic constant by 56fold and increase in the dissociation constant by 75fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis |
711310 |
| 1.1.1.50 | S114A/Y153F |
double mutation results in a significant decrease in kcat relative to the single mutant Y153F |
760734 |
| 1.1.1.50 | more |
enzyme silencing by specific siRNA suppresses 3alpha-HSD3 expression without interfering with 3alpha-HSD4, which shares a highly homologous active site, the 5alpha-DHT concentration increases, whereas MCF7 cell growth is suppressed |
740017 |
| 1.1.1.50 | D249K |
he mutation leads to 4fold increased Km value compared to the wild type, the mutant shows increased retention time, suggesting a smaller molecule size than dimeric wild type enzyme |
695886 |
