EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.50 | D249A |
mutation interrupts salt bridge between residues D249 and R167, secondary structure similar to wild-type. 30fold decrease in catalytic efficiency, decrease in melting temperature |
695886 |
| 1.1.1.50 | D249A |
the mutation leads to 2fold 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 |
| 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 |
| 1.1.1.50 | D249K |
mutation interrupts salt bridge between residues D249 and R167, secondary structure similar to wild-type. 1.4fold decrease in catalytic efficiency, decrease in melting temperature |
695886 |
| 1.1.1.50 | D249S |
mutation interrupts salt bridge between residues D249 and R167, secondary structure similar to wild-type. 1400fold decrease in catalytic efficiency, decrease in melting temperature |
695886 |
| 1.1.1.50 | D249S |
the mutant has similar kinetic parameters to wild type enzyme |
695886 |
| 1.1.1.50 | E276R |
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKR1C9 and its cofactor specificity, overview |
684676 |
| 1.1.1.50 | F118A |
site-directed mutagenesis, altered kinetic and catalytic efficiency compared to the wild-type enzyme |
656651 |
| 1.1.1.50 | F118A |
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 | F129A |
site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme, highly reduced activity |
655215 |
