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Results 1 - 8 of 8
EC Number Renatured (Commentary) Reference
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.150% of the wild-type enzyme is unfolded at 5.22 M urea. Mutant enzymes R72A, E118A, N120A and E118A/N120A are unfolded at lower concentrations 651806
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.170-87% refolding of recombinant C-terminally His6-tagged enzyme after expression in Escherichia coli as insoluble protein and solubilization by denaturation, detergent treatment, and 40fold dilution by a single-step column-based refolding step with an elution gradient, dilution with buffer 1% bovine serum albumin, 20 mM phosphate, 150 mM NaCl, optimal at pH 6.8, method optimization, overview 678842
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.1detection of an intermediate during the unfolding process of the dimeric ketosteroid isomerase, NMR spectroscopy, circular dichroism and fluorescence spectroscopies, and small angle X-ray scattering and analytical ultracentrifugation of native and fully unfolded enzymes, overview 679832
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.1dilution refolding of recombinant enzyme from inclusion bodies, denatured recombinant C-terminally His6-tagged enzyme 10fold with refolding buffer containing 50 mM potassium phosphate, pH 7.0, 4°C, incubation at 4°C for 12 h, urea 0.8 M 678846
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.1repeated adsorptive refolding in an expanded bed with gradient change in the feed-stream composition from denaturing buffer containing 8 M urea and 50 mM potassium phosphate, pH 6.8 to the refolding buffer containing 50 mM potassium phosphate, pH 6.8, constant liquid feed rate, method evaluation, overview 678900
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.1secondary structure is not significantly affected by urea up to 3.5 M, but the residues in the dimeric interface region are significantly perturbed by urea at low concentrations. The interface region primarily around the beta5- and beta6-strands may play an important role as the starting positions in the unfolding process 692914
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.1the recovery of the activity by refolding is not diminished even after a prolonged time, 24 h of exposure to 7 M urea 649932
Show all pathways known for 5.3.3.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.1urea-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 653790
Results 1 - 8 of 8