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Results 1 - 10 of 53 > >>
EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Commentary Reference
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1-999 - effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview 715948
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1-999 - effect of pH and temperature as function of time on stability of CAs from different species, overview 715948
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1-999 - the enzyme exhibits more than 80% stability between pH 7.0 and pH 8.0, while 68% and 57% are retained at pH 8.5 and pH 9.0 after 3 h of incubation. The enzyme retains 63%, 54% and 45% residual activity at pH 8.0, pH 8.5, and pH 9.0, respectively, following 6 h of incubation. Effect of pH and temperature as function of time on stability of CAs from different species, overview 715948
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1-999 - the thermal unfolding of recombinant BhCA is studied by using circular dichroism 747660
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1-999 - thermal stability and thermal unfolding analyses of wild-type enzyme and mutants M1-M4, overview 748739
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.130 - stable up to 652647
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.130 - the enzyme possesses two stable folded conformers with the conformational transition occurring at about 30°C. The methodology yields a stability curve for the complete unfolding of the enzyme below this temperature but only the partial unfolding, to the molten globule state, above it. The transition state thermodynamics for the low-term to physiological-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mole and the transition state possesses a substantial unfolding quality 680579
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.130 100 purified recombinant His-tagged enzyme lacking the signal peptide, pH 7.6, 15 min, slow decrease in the enzyme activity at temperatures up to 50°C and almost no effect beyond 50°C up to 100°C. The enzyme retains over 80% of its activity between 60°C and 100°C, the Tm is 84.5°C 749198
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.135 45 the purifed enzyme retains 38-54% after 6 h 715948
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.135 45 the purifed enzyme retains 40-51% after 6 h 715948
Results 1 - 10 of 53 > >>