Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.1.1 extracted from

  • Benitez-Cardoza, C.G.; Rojo-Dominguez, A.; Hernandez-Arana, A.
    Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein (2001), Biochemistry, 40, 9049-9058.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00942
-
-

Renatured (Commentary)

Renatured (Comment) Organism
the refolding reaction of the thermally denatured enzyme obeys second-order kinetics and leads to the formation of dimer nativelike enzyme, dimerization is coupled to the regain of a large amount of secondary structure Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
denaturation of the enzyme likely consists of an initial first-order reaction that forms thermally unfolded enzyme, followed by irreversibility-inducing reactions which are probably linked to aggregation of the unfolded protein Saccharomyces cerevisiae
63
-
if denaturation is carried out at temperatures above 64.0°C, a partially folded species is formed in a time short enough to avoid the occurence of deleterious aggregation reactions Saccharomyces cerevisiae