Literature summary for 5.3.3.1 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

Inhibitors	Comment	Organism	Structure
Urea	enzymatic activity is affected significantly by urea and decreases exponentially as urea concentration increases	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	biotype B	-

Renatured (Commentary)

Renatured (Comment)	Organism
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

Renatured (Comment)

Organism

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

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Release 2023.1 (January 2023)