EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.50 | K157A |
the NADH binding affinity of K157A mutant is much lower than that of the wild-type, mainly due to loss of a hydrogen bond |
760734 |
| 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 | 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 | K159A |
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 200fold reduced activity compared to the wild-type |
669389 |
| 1.1.1.50 | K159A |
site-directed mutagenesis, the mutation changes the rate-limiting step to the hydride transfer, proton transfer is blocked in the mutant but can be rescued using exogenous proton acceptors, such as buffers, small primary amines, and azide, overview |
687642 |
| 1.1.1.50 | K159M |
site-directed mutagenesis, the mutation changes the rate-limiting step to the hydride transfer, proton transfer is blocked in the mutant but can be rescued using exogenous proton acceptors, such as buffers, small primary amines, and azide, overview |
687642 |
| 1.1.1.50 | L54A |
site-directed mutagenesis, altered kinetic and catalytic efficiency compared to the wild-type enzyme |
656651 |
| 1.1.1.50 | L54A |
site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme |
655215 |
| 1.1.1.50 | more |
construction of insertion mutants, overview |
687870 |
| 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 |
