Enzyme Eyring equation

Figure 4 shows the temperature profiles for amidase activity of the protease from M. jannaschii at 10,250, and 500 atm. The optimum temperature for activity of 116° at low pressure (10 atm) is one of the highest optimum temperatures for a proteolytic enzyme reported in the literature. Figure 4 also shows that pressure substantially enhances the activity of the protease at each temperature for example, application of 500 atm increases the maximum reaction rate about twofold and the rate at 130°C fivefold. The 400% enhancement of amidase activity at 130° translates to an overall activation volume, A V, of — 106 ml mol , as determined by the Johnson-Eyring equation [Eq. (2)]. The most negative activation volumes previously reported for serine proteases were —36 ml mol for the digestion of casein by trypsin and —33 ml mol for the hydrolysis of Suc-Ala-Ala-pNA by a-chymotrypsin. Michels and Clark also found that the protease is stabilized... 

The effect of temperature on enzyme reactivity (expressed by the rate constant kcat or the parameter V) can be analyzed from the theory of the activated complex (or transition state theory, TST) or else by using the semi-empirical correlation of Arrhenius. According to TST (Rooney 1995), the equation of Eyring describes the effect of temperature on any rate constant ... 

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