Abstract
At low temperature (3°C), and in the absence of substrate and cofactor, the enzyme, fructose diphosphatase (FDPase), extracted from liver of the benthic fishCoryphaenoides acrolepis, is reversibly inactivated by exposure to relatively low pressures (5,000 psi). At pressures of 20,000 psi at 3°C the native enzyme is irreversibly denatured. When the cofactor and the substrate are present, the enzyme is protected against pressure denaturation; hence, catalysis is insensitive to at least 10,000 psi at 3°C. Similarly, interactions between FDPase and its negative modulator adenosine monophosphate (AMP), are largely pressure insensitive. Pressure sensitivity of the native enzyme and of the catalytic process is much reduced at temperatures above about 9°C. The homologous enzyme from a surface fish,Pimelometopon pulchrum, is strikingly more sensitive to pressure, particularly at low temperatures.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature cited
Behrisch, H. W.: Temperature and the regulation of enzyme activity in poikilotherms. Fructose diphosphatase from migrating salmon. Biochem. J.115, 687–696 (1969).
— andP. W. Hochachka: Temperature and the regulation of enzyme activity in poikilotherms. Properties of trout fructose-diphosphatase. Biochem. J.111, 287–295 (1969a).
——: Temperature and the regulation of enzyme activity in poikilotherms. Properties of lungfish fructose-diphosphatase. Biochem. J.112, 601–607 (1969b).
Brandts J. F., R. J. Oliveira andC. Westort: Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry N.Y.9, 1038–1047 (1970).
DeVault, D., A. Tasaki, P. Thornber and B. Chance: Effect of high hydrostatic pressure upon light-activated electron transfer and H3O+ binding inChromatium cells, chromatophores, and active center preparation. Biophys. J.10, 124a (Abstract) (1970).
Gevers, W. andH. A. Krebs: The effects of adenine nucleotides on carbohydrate metabolism in pigeon liver homogenates. Biochem. J.98, 720–735 (1966).
Gordon, M. S.: Hydrostatic pressure.In: Fish physiology, Vol.4. Ed. by W. Hoar, and D. Randall New York: Academic Press. (In press) (1970).
Hill, E. P. andR. Y Morita: Dehydrogenase activity under hydrostatic pressure by isolated mitochondria obtained fromAllomyces macrogynus. Limnol. Oceanogr.9, 243–248 (1964).
Hochachka, P. W., andG. N. Somero: Biochemical adaptation to the environment.In: Fish physiology, Vol.6. Ed. by W. S. Hoar and D. Randall. New York: Academic Press (1970). (In press)
Ikkai, T. andT. Ooi: The effects of pressure on actomyosin systems. Biochemistry N.Y.8, 2615–2622 (1969).
Knight-Jones, E. W. andE. Morgan: Responses of marine animals to changes in hydrostatic pressure. Oceanogr. mar. Biol. A. Rev.4, 267–299 (1966).
Koster, F. F. andC. Veeger: The relation between temperature-inducible allosteric effects and the activation energies of amino-acid ocidases. Biochem. Biophys. Acta167, 48–63 (1968).
Morita, R. Y.: Effects of hydrostatic pressure on marine micro organisms. Oceanogr. mar. Biol. A. Rev.5, 187–203 (1967).
Newsholme, E. A. andW. Gevers: Control of glycolysis and gluconeogenesis in liver and kidney cortex. Vitams Horm.25, 1–87 (1967).
Schlieper, C.: High pressure effects on marine invertebrates and fishes. Mar. Biol.2, 5–12 (1968).
Suzuki, C. andK. Kitamura: Inactivation of enzymes under high pressure. Studies of the kinetics of inactivation of α-amylase ofBacillus subtilis under high pressure. J. Biochem., Tokyo54, 214–219 (1963).
— andK. Suzuki: The protein denaturation by high pressure. Changes of optical rotation and susceptibility to enzymic proteolysis with ovalbumin denatured by pressure. J. Biochem., Tokyo52, 67–71 (1962).
Taketa, K. andB. Pogell: Allosteric inhibition of rat liver fructose 1, 6-diphosphatase by adenosine 5′ monophosphate. J. biol. Chem.240, 651–662 (1965).
Weber, G., R. L. Singhal andS. K. Srivastava: Action of glucocorticoid as inducer and insulin as suppressor of biosynthesis of hepatic gluconeogenic enzymes. Adv. Enz. Regul.4, 43–75 (1965).
Williamson, J. R., M. Peterson andS. Rostand: Use of 5-methyl pyrazole-3-carboxylic acid in studies on the mode of action of glucagon. Fedn Proc. Fedn Am. Socs exp. Biol.29, 735 (Abstract) (1970).
Zobell, C. E. andC. H. Oppenheimer: Some effects of hydrostatic pressure on the multiplication and the morphology of marine bacteria. J. Bact.60, 771–781 (1950).
Author information
Authors and Affiliations
Additional information
Communicated byT. R. Parsons, Nanaimo
Rights and permissions
About this article
Cite this article
Hochachka, P.W., Schneider, D.E. & Kuznetsov, A. Interacting pressure and temperature effects on enzymes of marine poikilotherms: Catalytic and regulatory properties of FDPase from deep and shallow-water fishes. Mar. Biol. 7, 285–293 (1970). https://doi.org/10.1007/BF00750821
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00750821