Summary
-
1.
Structural, kinetic and thermodynamic activation properties of muscle pyruvate kinases from invertebrate species adapted to different thermal environments were examined.
-
2.
Structural rigidity, as estimated by ammonium sulfate precipitation and heat inactivation temperature, is positively correlated with acclimatization temperature of the organism (Fig. 1).
-
3.
K m-values for PEP are hardly influenced by experimental temperatures within the normal temperature range of the species (Fig. 2). A good correlation, however, exists betweenK m-values and the capacity of tissues for aerobic glycolysis (Fig. 3).
-
4.
All pyruvate kinases can exist in two (or more) temperature-dependent conformational states. Sizes of ΔH≠-values are correlated with the species' acclimatization temperature (Fig. 6) but not with the temperature variability in the cells (Fig. 7).
-
5.
A correlation exists between the free energy of activation ΔG≠, body temperatures and the capacity of muscles for aerobic glycolysis (Table 2).
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- PK:
-
pyruvate kinase
- PEP:
-
phosphoenolpyruvate
- K m :
-
Michaelis constant
- ΔH≠:
-
enthalpy of activation
- ΔG≠:
-
free energy of activation
- ΔS≠:
-
entropy of activation
References
Altman, P.L., Dittmer, D.S.: Metabolism. Bethesda: Federation of American Societies for Experimental Biology 1968
Alexandrov, V.Y.: Conformational flexibility of proteins and their resistance to proteinases and temperature conditions of life. Curr. Mod. Biol.3, 9–19 (1969)
Baily, E., Stirpe, F., Taylor, C.B.: Regulation of rat liver pyruvate kinase. Biochem. J.108, 427–436 (1968)
Baldwin, J.: Selection for catalytic efficiency of lactate dehydrogenase M4: Correlation with body temperature and levels of anaerobic glycolysis. Comp. Biochem. Physiol.52B, 33–37 (1975)
Berkel, J.C. van, Koster, J.F., Hülsmann, W.C.: Two interconvertible forms of L-Type pyruvate kinase from rat liver. Biochim. biophys. Acta (Amst.)293, 118–124 (1973)
Carbonell, J., Felíu, J.E., Marco, R., Sols, A.: Pyruvate kinase: classes of regulatory isoenzymes in mammalian tissues. Europ. J. Biochem.37, 148–156 (1973)
Dowd, J.E., Riggs, D.S.: A comparison of estimates of Michaelis-Menten kinetic constants from various linear transformations. J. biol. Chem.240, 863–869 (1965)
Ghiretti, F.: Respiration. In: Physiology of mollusca (Wilburg, K.M., Yonge, C.M., eds.). New York-London: Academic Press 1966
Havsteen, B.: NADP+/Isocitrate dehydrogenase fromIdus idus (Pisces). III. Discussion of temperature dependence of kinetic parameters. Marine Biology25, 77–83 (1974)
Herter, K.: Der Temperatursinn der Insekten. Berlin: Duncker und Humblot 1953
Herter, K.: Der Temperatursinn der Tiere. Wittenberg 1962
Hochachka, P.W., Mustafa, T.: Invertebrate facultative anaerobiosis. Science178, 1056–1060 (1972)
Hochachka, P.W., Somero, G.N.: Strategies of biochemical adaptation. Philadelphia-London-Toronto: Saunders 1973
Hoffmann, K.H.: Pyruvate kinase from muscle and fat body of the house cricketAcheta domesticus L.: Purification and catalytic studies. J. comp. Physiol.104, 59–69 (1975)
Johnson, F.H., Eyring, H., Polissar, M.J.: The kinetic basis of molecular biology, p. 20. New York: Wiley and Chapman 1954
Künnemann, H.: Der Einfluß der Temperatur auf Thermostabilität, Isoenzymmuster und Reaktions-kinetik der Laktat-Dehydrogenase aus Fischen. Marine Biology18, 37–45 (1973)
Low, P.S., Bada, J.L., Somero, G.N.: Temperature adaptation of enzymes. Roles of free energy, the enthalpy, and the entropy of activation. Proc. nat. Acad. Sci. (Wash.)70, 430–432 (1973)
Low, P.S., Somero, G.N.: Temperature adaptation of enzymes: A proposed molecular basis for the different catalytic efficiencies of enzymes from ectotherms and endotherms. Comp. Biochem. Physiol.49B, 307–312 (1974)
Low, P.S., Somero, G.N.: Environmental adaptation of muscle pyruvate kinases: Kinetic and structural differences related to temperature and pressure. J. exp. Zool., in press (1976)
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol reagent. J. biol. Chem.193, 265–275 (1951)
Luisi, P.L., Baici, A., Olomucki, A., Doublet, M.O.: Temperature-determined enzymatic functions in octopine dehydrogenase. Europ. J. Biochem.50, 511–516 (1975)
Newell, R.C.: Factors affecting the respiration of intertidal invertebrates. Amer. Zool.13, 513–528 (1973)
Precht, H., Christophersen, J., Hensel, H., Larcher, W.: Temperature and life. Berlin-Heidelberg-New York: Springer 1973
Robert, M., Gray, I.: Enzymatic mechanisms during temperature acclimation of the blue crab,Callinectes sapidus. II. Kinetic and thermodynamic studies of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Comp. Biochem. Physiol.42B, 389–402 (1972)
Somero, G.N.: Enzymatic mechanisms of temperature compensation: Immediate and evolutionary effects of temperature on enzymes of aquatic poikilotherms. Amer. Naturalist103, 517–530 (1969)
Zwaan, A. de, Bont, A.M.Th. de: Phosphoenolpyruvate carboxykinase from adductor muscle tissue of the sea musselMytilus edulis L. J. comp. Physiol.96, 85–94 (1975)
Author information
Authors and Affiliations
Additional information
Supported by the Deutsche Forschungsgemeinschaft (Ho 631/1, Ho 631/2). Parts of this work have been carried out during a Research Studentship at Scripps Institution of Oceanography, University of California, La Jolla, USA. I am deeply obliged to Prof. Dr. G.N. Somero for scientific discussions and reading of this manuscript
Rights and permissions
About this article
Cite this article
Hoffmann, KH. Catalytic efficiency and structural properties of invertebrate muscle pyruvate kinases: Correlation with body temperature and oxygen consumption rates. J Comp Physiol B 110, 185–195 (1976). https://doi.org/10.1007/BF00689307
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00689307