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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.
    View publication on PubMedView publication on EuropePMC

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