Kinetic study on the irreversible thermal denaturation of Schistosoma japonicum glutathione s-transferase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 5, 2006, Pages 979-984

  Quesada Soriano, Indalecio ^a   García Maroto, Federico ^a   García Fuentes, Luis ^a  

^a Facultad de Ciencias Experimentales   (Spain)

Author keywords

Differential scanning calorimetry; Glutathione S transferase; Irreversible; Thermal denaturation

Indexed keywords

GLUTATHIONE TRANSFERASE; S HEXYLGLUTATHIONE;

ARTICLE; CONCENTRATION RESPONSE; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME KINETICS; ENZYME STABILITY; ENZYME SUBSTRATE; PH; PRIORITY JOURNAL; SCHISTOSOMA JAPONICUM; TEMPERATURE SENSITIVITY; THERMODYNAMICS; THERMOGRAPHY; THERMOSTABILITY;

ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; GLUTATHIONE TRANSFERASE; HEAT; HELMINTH PROTEINS; KINETICS; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SCHISTOSOMA JAPONICUM;

SCHISTOSOMA JAPONICUM;

EID: 33646501425     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.03.002     Document Type: Article

References (31)

1. Hayes J.D., Flanagan J.U., and Jowsey I.R. Glutathione transferases. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 51-88
2. Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16
3. Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Rüker F., and Carter D.C. Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3 (1994) 2233-2244
4. Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10 (1997) 2-18
5. Wallace L.A., Sluis-Cremer N., and Dirr H.W. Equilibrium and kinetic unfolding properties of dimeric human glutathione transferase A1-1. Biochemistry 37 (1998) 5320-5328
6. Erhardt J., and Dirr H. Native dimer stabilizes the subunit tertiary structure of porcine class pi glutathione S-transferase. Eur. J. Biochem. 230 (1995) 614-620
7. Aceto A., Caccuri A.M., Sacchetta P., Bucciarelli T., Dragani B., Rosato N., Federici G., and Di Ilio C. Dissociation and unfolding of Pi-class glutathione transferase. Evidence for a monomeric inactive intermediate. Biochem. J. 285 (1992) 241-245
8. Kaplan W., Husler P., Klump H., Erhardt J., Sluis-Cremer N., and Dirr H. Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag. Protein Sci. 6 (1997) 399-406
9. Ortiz-Salmerón E., Yassin Z., Clemente-Jimenez M.J., Las Heras-Vazquez F.J., Rodriguez-Vico F., Barón C., and García-Fuentes L. Thermodynamic analysis of the binding of glutathione to glutathione S-transferase over a range of temperatures. Eur. J. Biochem. 268 (2001) 4307-4314
10. Yassin Z., Clemente-Jimenez M.J., Téllez-Sanz R., and García-Fuentes L. Salt influence on glutathione-Schistosoma japonicum glutathione S-transferase binding. Int. J. Biol. Macromol. 31 (2003) 155-162
11. Yassin Z., Ortiz-Salmerón E., García-Maroto F., Barón C., and García-Fuentes L. Implications of the ligandin binding site on the binding of non-substrate ligands to Schistosoma japonicum-glutathione transferase. Biochim. Biophys. Acta 1698 (2004) 227-237
12. Simons P.C., and Van der Jagt D.L. Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography. Anal. Biochem. 82 (1977) 334-341
13. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
14. Perkins S.J. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering match points and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157 (1986) 169-180
15. Takahashi K., and Sturtevant J.M. Thermal denaturation of streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex. Biochemistry 20 (1981) 6185-6190
16. Sánchez-Ruiz J.M., López-Lacomba J.L., Cortijo M., and Mateo P.L. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 27 (1988) 1648-1652
17. Sánchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61 (1992) 921-935
18. Vogl T., Jatzke C., Hinz H.J., Benz J., and Hüber R. Thermodynamic stability of annexin V E17G: equilibrium parameters from an irreversible unfolding reaction. Biochemistry 36 (1997) 1657-1668
19. Thórólfsson M., Ibarra-Molero B., Fojan P., Petersen S.B.., Sánchez-Ruiz J.M., and Martínez A. L-phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study. Biochemistry 81 (2002) 7573-7585
20. Sayed Y., Wallace L.A., and Dirr H.W. The hydrophobic lock-and-key intersubunit motif of glutathione transferase A1-1: implications for catalysis, ligandin function and stability. FEBS Lett. 465 (2000) 169-172
21. Dirr H.W., and Reinemer P. Equilibrium unfolding of class pi glutathione S-transferase. Biochem. Biophys. Res. Commun. 180 (1991) 294-300
22. Kurganov B.I., Lyubarev A.E., Sánchez-Ruiz J.M., and Shnyrov V.L. Analysis of differential scanning calorimetry data for proteins. Criteria of validity of one-step mechanism of irreversible protein denaturation. Biophysical Chemistry 69 (1997) 125-135
23. Nielsen A.D., Pusey M.L., Fuglsang C.C., and Westh P. A proposed mechanism for the thermal denaturation of a recombinant Bacillus halmapalus α-amylase-the effect of calcium ions. Biochim. et Biophys. Acta 1652 (2003) 52-63
24. Zoldak G., Zubrik A., Musatov A., Stupak M., and Sedlak E. Irreversible thermal denaturation of glucose oxidase from Aspergillus niger is the transition to the denatured state with residual structure. J. Biol. Chem. 279 (2004) 47601-47609
25. Michnik A., Drzazga Z., Kluczewska A., and Michalik K. Differential scanning microcalorimetry study of the thermal denaturation of haemoglobin. Biophys. Chem. 118 (2005) 93-101
26. Lumry R., and Eyring H. Conformational changes of proteins. J. Phys. Chem. 58 (1954) 110-120
27. Lyubarev A.E., and Kurganov B.I. Modeling of irreversible thermal protein denaturation at varying temperature: I. The model involving two consecutive irreversible steps. Biochemistry (Mosc) 63 (1998) 434-440
28. Shnyrov V.L., Martínez L.D., Roig M.G., Lyubarev A.E., Kurganov B.I., and Villar E. Irreversible thermal denaturation of lipase B from Candida rugosa. Thermochim. Acta 325 (1999) 143-149
29. Lyubarev A.E., Kurganov B.I., Orlov V.N., and Zhou H.-M. Two-state irreversible thermal denaturation of muscle creatine kinase. Biophys. Chem. 79 (1999) 199-204
30. Ortiz-Salmerón E., Nuccetelli M., Oakley A.J., Parker M.W., Lo Bello M., and García-Fuentes L. Thermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathione. J. Biol. Chem. 278 (2003) 46938-46948
31. Ortiz-Salmerón E., Yassin Z., Clemente-Jimenez M.J., Las Heras-Vázquez F.J., Rodríguez-Vico F., Barón C., and García-Fuentes L. A calorimetric study of the binding of S-alkylglutathiones to glutathione S-transferase. Biochim. Biophys. Acta 1548 (2001) 106-113