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