Inhibitors | Comment | Organism | Structure |
---|---|---|---|
guanidine hydrochloride | guanidine hydrochloride-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Complete inhibition at 0.4 M | Wolbachia endosymbiont of Brugia malayi | |
Urea | urea-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Complete inhibition at 1.0 M | Wolbachia endosymbiont of Brugia malayi |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Wolbachia endosymbiont of Brugia malayi | Q5GTD5 | - |
- |
Wolbachia endosymbiont of Brugia malayi TRS | Q5GTD5 | - |
- |
Renatured (Comment) | Organism |
---|---|
guanidine hydrochloride and urea-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Thymidylate kinase is more prone to ionic perturbation | Wolbachia endosymbiont of Brugia malayi |
Subunits | Comment | Organism |
---|---|---|
More | the dimeric assembly of thymidylate kinase is an absolute requirement for enzymatic activity and any subtle change in dimeric conformation due to denaturation leads to loss of enzymatic activity | Wolbachia endosymbiont of Brugia malayi |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3 | 4 | about 100-70% loss of structure | Wolbachia endosymbiont of Brugia malayi |
5 | 8 | structurally and functionally stable | Wolbachia endosymbiont of Brugia malayi |
9 | 10 | about 30-40% loss of structure | Wolbachia endosymbiont of Brugia malayi |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
155 | - |
pH 7.4, 37°C | Wolbachia endosymbiont of Brugia malayi | guanidine hydrochloride | |
600 | - |
pH 7.4, 37°C | Wolbachia endosymbiont of Brugia malayi | Urea |