Literature summary for 5.3.1.1 extracted from

Tellez, L.A.; Blancas-Mejia, L.M.; Carrillo-Nava, E.; Mendoza-Hernandez, G.; Cisneros, D.A.; Fernandez-Velasco, D.A.
Thermal unfolding of triosephosphate isomerase from Entamoeba histolytica: dimer dissociation leads to extensive unfolding (2008), Biochemistry, 47, 11665-11673.

Organism

Organism	UniProt	Comment	Textmining
Entamoeba histolytica	O02611	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
study on thermal dissociation and unfolding of enzyme and a monomeric variant obtained by chemical derivatization. During wild-type unfolding, sequential transitions corresponding to dimer dissociation into a compact monomeric intermediate followed by unfolding and further aggregation of the intermediate occurr. In the case of the monomeric variant, a single transition, analogous to the second transition of wild-type, is observed. Dimer dissociation is not restricted to localized interface reorganization. Dissociation represents 55% of the total enthalpy change. Subunit assembly is probably best represented by a fly-casting mechanism	Entamoeba histolytica

Renatured (Comment)

Organism

study on thermal dissociation and unfolding of enzyme and a monomeric variant obtained by chemical derivatization. During wild-type unfolding, sequential transitions corresponding to dimer dissociation into a compact monomeric intermediate followed by unfolding and further aggregation of the intermediate occurr. In the case of the monomeric variant, a single transition, analogous to the second transition of wild-type, is observed. Dimer dissociation is not restricted to localized interface reorganization. Dissociation represents 55% of the total enthalpy change. Subunit assembly is probably best represented by a fly-casting mechanism

Entamoeba histolytica

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Release 2023.1 (January 2023)