Interacting pressure and temperature effects on enzymes of marine poikilotherms: Catalytic and regulatory properties of FDPase from deep and shallow-water fishes

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.