Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve?
Answer to relevant QuestionsHow do the KM values for glucoki-nase and hexokinase reflect their roles in sugar metabolism? What is the difference between pure and mixed noncompetitive inhibition? Is it good (or bad) that enzymes can be reversibly inhibited? Why? Explain how glycogen phosphorylase is controlled allosterically and by covalent modification. What is the relationship between a transition-state analog and the induced-fit model of enzyme kinetics?
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