Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model.
Enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface of several organisms, among other functions. Despite its participation in a variety of biological and pathophysiological processes, its stability and folding/unfolding reaction have not been fully explored. In this paper we present, the urea and GdnHCl-induced denaturation of enolase studied by means of fluorescence and circular dichroism spectroscopies. We found that enolase unfolds through a highly reversible pathway, populating a stable intermediate species in a range of experimental conditions. The refolding reaction also exhibits an intermediate state that might have a slightly more compact conformation compared to the unfolding intermediate. The thermodynamic parameters associated with the unfolding reaction are presented and discussed.
Sánchez-Miguel
Dénison S
DS
Laboratorio de Investigación Bioquímica, Programa Institucional en Biomedicina Molecular, Sección de Estudios de Posgrado, ENMyH-Instituto Politécnico Nacional, Guillermo Massieu Helguera No. 239, La Escalera Ticoman, DF, 07320, Mexico.
Romero-Jiménez
Jahir
J
Reyes-López
César A
CA
Cabrera-Avila
Ana Lilia
AL
Carrillo-Ibarra
Normande
N
Benítez-Cardoza
Claudia G
CG
D007700:Kinetics; D008958:Models, Molecular; D010751:Phosphopyruvate Hydratase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
D029701:Saccharomyces cerevisiae Proteins; D010751:Phosphopyruvate Hydratase