2.7.4.25	D132A	site directed mutagenesis	676227	
2.7.4.25	D132A	the mutant shows reduced activity compared to the wild type enzyme, the mutation has the most dramatic consequences on the protein stability as Tm decreases by 9°C in comparison with the wild type protein, an increase in the specificity of the D132A variant for UMP over CMP and dCMP is observed	692282	
2.7.4.25	D132A	the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP	692282	
2.7.4.25	D132H	site directed mutagenesis	676227	
2.7.4.25	D132H	the mutant shows reduced activity compared to the wild type enzyme	692282	
2.7.4.25	D132H	the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP, the D132H variant does not introduce charge reversal, because His is calculated to be deprotonated	692282	
2.7.4.25	D132N	site directed mutagenesis	676227	
2.7.4.25	D132N	the mutant shows reduced activity compared to the wild type enzyme	692282	
2.7.4.25	D132N	the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP	692282	
2.7.4.25	D132S	site directed mutagenesis	676227