Abstract
Kinetic study of the mechanism of the temperature-induced loss of the catalytic activity by yeast hexokinase (HK) and yeast glucose-6phosphate dehydrogenase (G-6-PDG) has shown the dissociative nature of the processes. In the temperature range 40–47°C, they are satisfactorily described in terms of consecutive reactions in which steps of irreversible denaturation of the monomeric units follow the reversible dissociation of inactive oligomeric forms into the active units, resulting in an increase in catalytic activity. The experimental data have been analyzed in the framework of the dissociative mechanism, and a semiquantitative method has been developed for calculating the individual rate constants.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Poltorak, O. M. and Chukrai, E. S. (1987), inModern Problems of Biokinetics. Moscow University, pp. 119–149.
Braginskaya, F. I, Zaitzeva, E. A., Zorina, O. M., Poltorak, O. M., Chukrai, E. S., and Dunn, F. (1990),Radiat. Environ. Biophys. 29, 48–56.
Kurganov, B.I. (1978),Allosteric Enzymes Moscow, pp. 67–110, Nauka.
Furman, T. C. and Neet, K. E. (1983),J. Biol. Chem. 258, 4930–4936.
Neet, K. E., Furman, T. C, and Hueston, W. J. (1982),Arch. Biochem. Biopys. 213, 14–19.
Yue, R. H., Noltman, E. A., and Kuby, S. A. (1969),J. Biol. Chem. 244, 1353–1364.
Luzzaatto, L. (1967),Biochem. Biophys. Acta 146, 18–25.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Zaitzeva, E.A., Chukria, E.S. & Poltorak, O.M. Thermostability of yeast hexokinase and yeast glucose-6-phosphate dehydrogenase. Appl Biochem Biotechnol 61, 67–74 (1996). https://doi.org/10.1007/BF02785689
Issue Date:
DOI: https://doi.org/10.1007/BF02785689