EC Number |
Protein Variants |
Reference |
---|
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 |
2.7.4.25 | D132A |
site directed mutagenesis |
676227 |
2.7.4.25 | D132H |
site directed mutagenesis |
676227 |
2.7.4.25 | D132N |
site directed mutagenesis |
676227 |
2.7.4.25 | D132S |
site directed mutagenesis |
676227 |
2.7.4.25 | R110M |
site directed mutagenesis |
676227 |
2.7.4.25 | R188M |
site directed mutagenesis |
676227 |
2.7.4.25 | S36A |
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 |