Literature summary for 3.4.22.69 extracted from

Chang, H.; Chou, C.; Chang, G.
Reversible unfolding of the severe acute respiratory syndrome coronavirus main protease in guanidinium chloride (2007), Biophys. J., 92, 1374-1383.

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Organic Solvent Stability

Organic Solvent	Comment	Organism
guanidine-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	Severe acute respiratory syndrome-related coronavirus

Organism

Organism	UniProt	Comment	Textmining
Severe acute respiratory syndrome-related coronavirus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
reversible unfolding of SARS-CoV main protease in guanidine-HCl. In the presence of 6 M of guanidine-HCl, the enzyme is completely unfolded in 10 min. The unfolding is completely reversible. A 10fold dilution induces refolding of the enzyme to a yield of 92-95%	Severe acute respiratory syndrome-related coronavirus

Synonyms

Synonyms	Comment	Organism
SARS main protease	-	Severe acute respiratory syndrome-related coronavirus

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Release 2023.1 (January 2023)