Effect of a specific inhibitor on the unfolding and refolding kinetics of dimeric triosephosphate isomerase: Establishing the dimeric and similarly structured nature of the main transition states on the forward and backward reactions

Biophysical Chemistry

Volumn 125, Issue 1, 2007, Pages 172-178

  González Mondragón, Edith ^a   Zubillaga, Rafael A ^a   Hernández Arana, Andrés ^a  

^a DEPARTAMENTO DE QUÍMICA   (Mexico)

Author keywords

Dimeric transition state; Inhibitor binding; Refolding kinetics; Unfolding kinetics; Unfolding transition state

Indexed keywords

2 PHOSPHOGLYCOLATE; ISOMERASE INHIBITOR; LIGAND; MONOMER; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; CONCENTRATION (PARAMETERS); KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; THERMODYNAMICS;

CIRCULAR DICHROISM; DIMERIZATION; GLYCOLATES; KINETICS; MATHEMATICS; PROTEIN FOLDING; PROTEIN RENATURATION; SACCHAROMYCES CEREVISIAE; TRIOSE-PHOSPHATE ISOMERASE;

EID: 33750718135     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.07.007     Document Type: Article

References (14)

1. Benítez-Cardoza C.G., Rojo-Domínguez A., and Hernández-Arana A. Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein. Biochemistry 40 (2001) 9049-9058
2. Vázquez-Contreras E., Zubillaga R.A., Mendoza-Hernández G., Costas M., and Fernández-Velasco D.A. Equilibrium unfolding of yeast triosephosphate isomerase: a monomeric intermediate in guanidine-HCl and two-state behavior in urea. Prot. Peptide Letters 7 (2000) 57-64
3. Morgan C.J., Wilkins D.K., Smith L.J., Yasushi K., and Dobson C.M. A compact monomeric intermediate identified by NMR in the denaturation of dimeric triosephosphate isomerase. J. Mol. Biol. 300 (2000) 11-16
4. Martel A., and Garel J.R. Renaturation of the allosteric phosphofructokinase from Escherichia coli. J. Biol. Chem. 259 (1984) 4917-4921
5. 2+ binding on the folding kinetics of alpha-lactalbumin. J. Mol. Biol. 206 (1989) 547-561
6. Sancho J., Meiering E.M., and Fersht A.R. Mapping transition states of protein unfolding by protein engineering of ligand-binding sites. J. Mol. Biol. 221 (1991) 1007-1014
7. Garel J.R., and Baldwin R.L. Both the fast and slow refolding reactions of ribonuclease A yield native enzyme. Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 3347-3351
8. Segawa S.I., and Sugihara M. Characterization of the transition state of lysozyme unfolding: II. Effects of the intrachain crosslinking and the inhibitor binding on the transition state. Biopolymers 23 (1984) 2489-2498
9. Chiti F., Taddei N., van Nuland N.A.J., Magherini F., Stefani M., Ramponi G., and Dobson C.M. Structural characterization of the transition state for folding of muscle acylphosphatase. J. Mol. Biol. 283 (1998) 893-903
10. González-Mondragón E., Zubillaga R.A., Saavedra E., Chánez-Cárdenas M.E., Pérez-Montfort R., and Hernández-Arana A. Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability. Biochemsitry 43 (2004) 3255-3263
11. Norton I.L., and Hartman F.C. Haloacetol phosphates, a comparative study of the active site of yeast and muscle triosephosphate isomerase. Biochemistry 11 (1972) 4435-4441
12. Schellman J.A. Macromolecular binding. Biopolymers 14 (1975) 999-1018
13. Jones R.B., and Waley S.G. Spectrophotometric studies on the interaction between triose phosphate isomerase and inhibitors. Biochem. J. 179 (1979) 623-630
14. Lambeir A.M., Opperdoes F.R., and Wierenga R.K. Kinetic properties of triose phosphate isomerase from Trypanosoma brucei. A comparison with the rabbit muscle and yeast enzymes. Eur. J. Biochem. 168 (1987) 69-74