Thermally induced changes in the structure and activity of yeast hexokinase B

Biophysical Chemistry

Volumn 137, Issue 2-3, 2008, Pages 88-94

  Ramshini, Hassan ^a   Rezaei Ghaleh, Nasrollah ^a   Ebrahim Habibi, Azadeh ^a   Saboury, Ali Akbar ^a   Nemat Gorgani, Mohsen ^a,b  

^a UNIVERSITY OF TEHRAN   (Iran)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Aggregation; Deamidation; Size exclusion HPLC; Thermoinactivation; Yeast hexokinase B

Indexed keywords

CYSTEINE; HEXOKINASE; HEXOKINASE ISOENZYME; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; DEAMINATION; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HIGH TEMPERATURE; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; TEMPERATURE DEPENDENCE; THERMOSTABILITY; YEAST;

AMIDES; CASEINS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CYSTEINE; DITHIOTHREITOL; ENZYME STABILITY; GAMMA-CYCLODEXTRINS; HEXOKINASE; HOT TEMPERATURE; ISOENZYMES; PROTEIN DENATURATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TRANSITION TEMPERATURE;

EID: 51649100449     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.07.004     Document Type: Article

References (50)

1. Kabsch W., and Holmes K.C. The actin fold. FASEB J. 9 (1995) 167-174
2. Wilson J.E. Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. J. Exp. Biol. 206 (2003) 2049-2057
3. Colowick S.P. The Enzymes (1973), Academic Press, New York
4. Kuser P.R., Krauchenco S., Antunes O.A.C., and Polikarpov I. The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into its mechanism of action. J. Biol. Chem. 275 (2000) 20814-20821
5. Anderson C.M., Stenkamp R.E., and Steitz T.A. Sequencing a protein by X-ray crystallography. II. Refinement of yeast hexokinase B co-ordinates and sequence at 2.1 A resolution. J. Mol. Biol. 123 (1978) 15-33
6. Bennett W.S., and Steitz T.A. Glucose-induced conformational change in yeast hexokinase. Proc. Natl. Acad. Sci. U.S.A. 75 (1978) 4848-4852
7. Shoham M., and Steitz T.A. The 6-hydroxymethyl group of a hexose is essential for the substrate-induced closure of the cleft in hexokinase. Biochem. Biohys. Acta 705 (1982) 380-384
8. Steitz T.A., Anderson W.F., Fletterick R.J., and Anderson C.M. High resolution crystal structures of yeast hexokinase complexes with substrates, activators, and inhibitors. Evidence for an allosteric control site. J. Biol. Chem. 252 (1977) 4494-4500
9. Anderson C.M., McDonald R.C., and Steitz T.A. Sequencing a protein by X-ray crystallography. I. Interpretation of yeast hexokinase B at 2.5 A resolution by model building. J. Mol. Biol. 123 (1978) 1-13
10. Feldman I., and Kramp D.C. Fluorescence-quenching study of glucose binding by yeast hexokinase isoenzymes. Biochemistry 17 (1978) 1541-1547
11. Ohning G.V., and Neet K.E. 6-(p-toluidinyl)naphthalene-2-sulfonic acid as a fluorescent probe of yeast hexokinase: conformational states induced by sugar and nucleotide ligands. Biochemistry 22 (1983) 2986-2995
12. Shill J.P., Peters B.A., and Neet K.E. Monomer-dimer equilibria of yeast hexokinase during reacting enzyme sedimentation. Biochemistry 13 (1974) 3864-3871
13. Womack F., and Colowick S.P. Catalytic activity with associated and dissociated forms of the yeast hexokinases. Arch. Biochem. Biophys. 191 (1978) 742-747
14. Schulze I.T., and Colowick S.P. The modification of yeast hexokinases by proteases and its relationship to the dissociation of hexokinase into subunits. J. Biol. Chem. 244 (1969) 2306-2316
15. Schmidt J.J., and Colowick S.P. Chemistry and subunit structure of yeast hexokinase isoenzymes. Arch. Biochem. Biophys. 158 (1973) 458-470
16. Gancedo J.M., Clifton D., and Fraenkel D.G. Yeast hexokinase mutants. J. Biol. Chem. 252 (1977) 4443-4444
17. Entian K.D. Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Mol. Gen.Genet. 178 (1980) 633-637
18. Dewinde J.H., Crauwels M., Hohmann S., Thevelein J.M., and Winderickx J. Differential requirement of the yeast sugar kinases for sugar sensing in establishing the catabolite-repressed state. Eur. J. Biochem. 241 (1996) 633-643
19. Shill J.P., and Neet K.E. A slow transient kinetic process of yeast hexokinase. Bichem. J. 123 (1971) 283-285
20. Kosowo D.P., and Rose I.A. Activators of yeast hexokinase. J. Biol. Chem. 246 (1971) 2618-2625
21. Marcus D.L., deLeon M.J., and Goldman J. Altered glucose metabolism in microvessels from patients with Alzheimer's disease. Ann. Neurol. 26 (1989) 91-94
22. Antuono P.G., Ravanelli-Meyer J., Nicholson K., and Bloom A.S. Leukocyte hexokinase activity in aging and Alzheimer disease. Dementia 6 (1995) 200-204
23. Arora K.K., and Pedersen P.L. Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP. J. Biol. Chem. 263 (1988) 17422-17428
24. Arora K.K., Fanciulli M., and Pedersen P.L. Glucose phosphorylation in tumor cells. Cloning, sequencing, and overexpression in active form of a full-length cDNA encoding a mitochondrial bindable form of hexokinase. J. Biol. Chem. 265 (1990) 6481-6488
25. White T.K., Kim J.Y., and Wilson J.E. Differential scanning calorimetric study of rat brain hexokinase: domain structure and stability. Arch. Biochem. Biophys. 276 (1990) 510-517
26. Catanzano F., Gambuti A., Graziano G., and Barone G. Interaction with d-glucose and thermal denaturation of yeast hexokinase B: a DSC study. J. Biochem. 121 (1997) 568-577
27. Tiwari A., and Bhat R. Stabilization of yeast hexokinase A by polyol osmolytes: correlation with the physicochemical properties of aqueous solutions. Biophys. Chem. 124 (2006) 90-99
28. Kaji A., Trayser K.A., and Colowick S.P. Multiple forms of yeast hexokinase. Ann. N. Y. Acad. Sci. 94 (1961) 798-811
29. Rezaei-Ghaleh N., Ramshini H., Ebrahim-Habibi A., Moosavi-Movahedi A.A., and Nemat-Gorgani M. Thermal aggregation of alpha-chymotrypsin: role of hydrophobic and electrostatic interactions. Biophys. Chem. 132 (2008) 23-32
30. Kurganov B.I., Rafikova E.R., and Dobrov E.N. Kinetics of thermal aggregation of tobacco mosaic virus coat protein. Biochemistry (Mosc) 67 (2002) 525-533
31. Laemmeli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
32. Khajeh K., and Nemat-Gorgani M. Comparative studies on a mesophilic and a thermophilic alpha-amylase. Appl. Biochem. Biotechnol. 90 (2001) 47-55
33. Kumar D.P., Tiwari A., and Bhat R. Effect of pH on stability and structure of yeast hexokinase A. J. Biol. Chem. 279 (2004) 32093-32099
34. Lepock J.R., Ritchie K.P., Kolios M.C., Rodhal A.M., Heinz K.A., and Kruuv J. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry. 31 (1992) 12706-12712
35. Tomazic S.J., and Klibanov A.M. Why is one Bacillus alpha-amylase more resistant against irreversible thermoinactivation than another?. J. Biol. Chem. 263 (1988) 3092-3096
36. Duy C., and Fitter J. Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics. J. Biol. Chem. 280 (2005) 37360-37365
37. Morales F.C., and Bianconi M.L. Influence of the oligomeric state of yeast hexokinase isozymes on inactivation and unfolding by urea. Biophys. Chem. 91 (2001) 183-190
38. Guerra R., and Bianconi M.L. Increased and catalytic efficiency of yeast hexokinase upon interaction with zwitterionic micelles kinetics and conformational studies. Biosci. Rep. 20 (2000) 41-48
39. Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (2001) 1-43
40. Tomazic S.J., and Klibanov A.M. Mechanisms of irreversible thermal inactivation of Bacillus alpha-amylases. J. Biol. Chem. 263 (1988) 3086-3091
41. Otieno S., Bhargava A.K., Serelis D., and Barnard E.A. Evidence for a single essential thiol in the yeast hexokinase molecule. Biochemistry 16 (1977) 4249-4255
42. Wright H.T. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol. 26 (1991) 1-52
43. Steitz T.A., Fletterick R.J., Anderson W.F., and Anderson Ch.M. High resolution X-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits. J. Mol. Biol. 104 (1976) 197-222
44. Anderson C.M., Zucker F.H., and Steitz T.A. Space-filling models of kinase clefts and conformation changes. Science 204 (1979) 375-380
45. Flaugh S.L., Mills I.A., and King J. Glutamine deamidation destabilizes human gamma D-crystallin and lowers the kinetic barrier to unfolding. J. Biol. Chem. 281 (2006) 30782-30793
46. Baldwin R.L. Intermediates in protein folding reactions and the mechanism of protein folding. Annu. Rev. Biochem. 44 (1975) 453-475
47. Zhang X., Fu X., Zhang H., Liu C., Jiao W., and Chang Z. Chaperone-like activity of beta-casein. Int. J. Biochem. Cell. Biol. 37 (2005) 1232-1240
48. Lee M.J., and Fennema O.R. Ability of cyclodextrins to inhibit aggregation of beta-casein. J. Agric. Food. Chem. 39 (1991) 17-21
49. Rozema D., and Gellman S.H. Artificial chaperone-assisted refolding of carbonic anhydraseB. J. Biol. Chem. 271 (1996) 3478-3487
50. Daugherty D.L., Rozema D., Hanson P.E., and Gellman S.H. Artificial chaperone-assisted refolding of citrate synthase. J. Biol. Chem. 273 (1998) 33961-33971