Summarize the effect of ion concentration on enzyme activity. Explain the mechan

Question

Summarize the effect of ion concentration on enzyme activity. Explain the mechanisms that cause this effect. b. Draw an "idealized" graph to illustrate the relationship between ion concentration and rate of enzyme activity. After an enzyme is mixed with its substrate, the amount of product formed is determined at 10-second intervals for 1 minute. Data from this experiment are shown below. a. What is the initial rate of this enzymatic reaction? ___ Show your calculation: b. What is the rate after 50 seconds? ___ Show your calculation: c. Why is the rate after 50 seconds different from the initial rate?

Explanation / Answer

For the given enzymatic reaction,

a. The initial rate of reaction = (0.25-0)/(10-0)

                                              = 0.025 mg/s

b. The rate after 50 s would be,

= (0.85 - 0)/(50-0)

= 0.085 mg/s

c. We see a difference in the rate of initial and final reaction because the enzyme sites are saturated and we get maximum rate at this point. The initial reaction with enzymes is lock-and-go type where enzyme binds to substrate but not all of it reacts and thus rate of product formation is low. At 50s all of enzymes sites are occupied and we get maximum product formation.

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