EC Number   |
Protein Variants |
Reference |
|---|
   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 |
