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	
2.7.4.25	D132S	the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP	692282	
2.7.4.25	D185A	the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme	712736	
2.7.4.25	R110M	site directed mutagenesis	676227	
2.7.4.25	R110M	the mutant shows reduced activity compared to the wild type enzyme	692282	
2.7.4.25	R110M	the side chains of Arg110 cannot establish hydrogen bonds with UMP, and its substitution by hydrophobic amino acids simultaneously affects the Km of CMP/dCMP and the kcat value	692282	
2.7.4.25	R181M	the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme	712736	
2.7.4.25	R188M	replacement of Arg188 with Met does not affect enzyme stability but dramatically decreases the kcat/Km ratio compared to the wild-type enzyme	692282	
2.7.4.25	R188M	site directed mutagenesis	676227	
2.7.4.25	R188M	the mutation does not affect enzyme stability but dramatically decreases the kcat_Km ratio compared with wild type enzyme, the mutant has no activity towards UMP	692282	
2.7.4.25	S101A	the mutation reduces CMP phosphorylation only moderately, but dramatically reduces dCMP phosphorylation	712736	
2.7.4.25	S36A	site directed mutagenesis	676227	
2.7.4.25	S36A	the S36A substitution mainly changes the Km value for the two natural substrates, which increases by a factor of 70 (CMP) and 37 (dCMP) compared with the parent molecule and decreases kcat of 1.6fold (CMP) and 7.4fold (dCMP) with respect to the wild type enzyme	692282	
2.7.4.25	S36A	the side chains of Arg110 cannot establish hydrogen bonds with UMP, and its substitution by hydrophobic amino acids simultaneously affects the Km of CMP/dCMP and the kcat value	692282	
2.7.4.25	V164E	substitution of Val164 by a Glu residue apparently does not affect the catalytic properties of Escherichia coli CMP kinase	645154