Literature summary extracted from
Kim, D.H.; Nam, G.H.; Jang, D.S.; Yun, S.; Choi, G.; Lee, H.C.; Choi, K.Y.
Roles of dimerization in folding and stability of ketosteroid isomerase from Pseudomonas putida biotype B (2001), Protein Sci., 10, 741-752.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
5.3.3.1 |
Urea |
enzymatic activity is affected significantly by urea and decreases exponentially as urea concentration increases |
Pseudomonas putida |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.3.3.1 |
Pseudomonas putida |
- |
biotype B |
- |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
5.3.3.1 |
urea-induced equilibrium unfolding, two-state mechanism involving only the native dimer and the unfolded monomer. The enzymatic activity is affected significantly by urea and decreases exponentially as urea concentration increases, suggesting that the active site is less stable than the tertiary structure as a whole. Dilution of the unfolded protein in 8 M urea to lower urea concentrations in a reducing condition, the activity of the refolded protein is recovered up to over 95% of that of the native protein. The protein folds into a monomer containing most of the alpha-helical structures before dimerization |
Pseudomonas putida |