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EC Number Organic Solvent Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.69guanidine-HCl dimeric enzyme dissociates at guanidinium chloride concentration of less than 0.4 M, at which the enzymatic activity loss showes close correlation with the subunit dissociation. Further increase in guanidinium chloride induces a reversible biphasic unfolding of the enzyme. The unfolding of the C-terminal domain-truncated enzyme follows a monophasic unfolding curve. Unfolding curves of mutants of the full-length protease W31 and W207/W218 are monophasic but correspond to the first and second phases of the protease, respectively. The unfolding intermediate of the protease represents a folded C-terminal domain but an unfolded N-terminal domain, which is enzymatically inactive due to loss of regulatory properties 678728
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.69more the enzyme activity is unaffected by Brij-35, Triton X-100 and Tween 20 or SDS 717308
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