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Chapter 12: Q4. (page 373)
Derive the Michaelis鈥揗enten equation.
The Michaelis-Menten equation is.
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Explain why it is usually easier to calculate an enzyme鈥檚 reaction velocity from the rate of appearance of product rather than the rate of disappearance of a substrate.
Why might an enzyme鈥檚 substrate, transition state, and product all serve as starting points for the design of a competitive inhibitor?
For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absenceof the inhibitor. The KM value is unchanged. (a) What type of inhibition is likely occurring? (b) What proportion of the enzyme molecules have bound inhibitor? (c) Calculate the inhibition constant.
What distinguishes an inhibitor from an inactivator?
Identify the enzymes in Table 12-1 whose catalytic efficiencies are near the diffusion-controlled limit.
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