Literature summary for 5.3.1.1 extracted from

Vazquez-Perez, A.R.; Fernandez-Velasco, D.A.
Pressure and denaturants in the unfolding of triosephosphate isomerase: the monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica (2007), Biochemistry, 46, 8624-8633.

Organism

Organism	UniProt	Comment	Textmining
Entamoeba histolytica	-	-	-
Saccharomyces cerevisiae	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Entamoeba histolytica. Monomer unfolding is reversible for both enzymes, the dissociation step is reversible in yeast and irreversible in Entamoeba histolytica. Monomer unfolding induced by high pressure in presence of guanidinium hydrochloride is reversible. In the absence of denaturants, pressure would induce monomer unfolding prior to dimer dissociation	Saccharomyces cerevisiae
study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Saccharomyces cerevisiae. Monomer unfolding is reversible for both enzymes, the dissociation step is reversible in yeast and irreversible in Entamoeba histolytica. Monomer unfolding induced by high pressure in presence of guanidinium hydrochloride is reversible. In the absence of denaturants, pressure would induce monomer unfolding prior to dimer dissociation	Entamoeba histolytica

Renatured (Comment)

Organism

study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Entamoeba histolytica. Monomer unfolding is reversible for both enzymes, the dissociation step is reversible in yeast and irreversible in Entamoeba histolytica. Monomer unfolding induced by high pressure in presence of guanidinium hydrochloride is reversible. In the absence of denaturants, pressure would induce monomer unfolding prior to dimer dissociation

Saccharomyces cerevisiae

study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Saccharomyces cerevisiae. Monomer unfolding is reversible for both enzymes, the dissociation step is reversible in yeast and irreversible in Entamoeba histolytica. Monomer unfolding induced by high pressure in presence of guanidinium hydrochloride is reversible. In the absence of denaturants, pressure would induce monomer unfolding prior to dimer dissociation

Entamoeba histolytica

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Release 2023.1 (January 2023)