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EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.851 - melting temperature, apo-enzyme 749805
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.859 - melting temperature, presence of copper 749805
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.861 - melting temperature, presence of 350 mM NaCl 749805
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.866 85 incubation of CopA in the absence of substrates at temperatures in the 66–85°C range leads to an irreversible exponential decrease in enzyme activity suggesting a two-state process involving fully-active and inactive molecules. Although CopA inactivated much slower than mesophilic proteins, the activation energy is similar to that observed for mesophilic P-type ATPases. The inactivation process is found to be associated with the irreversible partial unfolding of the polypeptide chain. However, the inactive thermally denatured protein still conserves large hydrophobic regions and considerable secondary structure 721417
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.875 - complete and irreversible inactivation after 70 min 721417
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