Some kinetic features of the hydrolysis of L-asparagine withE. coli asparaginase
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The influence of various effectors (methanol, neutral salts) on the kinetic parameters KM and kcat has been studied. The hypothesis has been expressed that chloride ions are responsible for the worsening of the binding of the substrate to the enzyme. The temperature dependence of the kinetic parameters KM and kcat for the enzymatic hydrolysis of L-asparagine has been obtained. It has been shown that the graph of log kcat versus 1/T has a break at 30°C. The effective activation energies below and above the critical point are 6.5 and 3.6 kcal/mole, respectively.
KeywordsKinetic Parameter Enzymatic Hydrolysis Chymotrypsin Asparaginase Effective Activation Energy
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