Literature summary for 5.3.1.1 extracted from

Najera, H.; Costas, M.; Fernandez-Velasco, D.A.
Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme (2003), Biochem. J., 370, 785-792.

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Organic Solvent Stability

Organic Solvent	Comment	Organism
guanidine-HCl	6 M, incubation times longer thah 10 min lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme	Saccharomyces cerevisiae
urea	8 M, incubation times longer than 5 h lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
reversible denaturation and renaturation of the homodimeric enzyme induced by urea and guanidine-HClm renaturation is fully reversible. Unfolding experiments do not reach an equilibrium, owing to a very slow dissociation and/or unfolding process. By contrast, equilibrium is reached in the refolding direction	Saccharomyces cerevisiae

Subunits

Subunits	Comment	Organism
dimer	the low stability of the monomers is neither the only, nor the main, cause for the dimeric nature of the enzyme	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)