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Chapter 12: Q25P (page 399)

You are constructing a velocity versus [substrate] curve for an enzyme whose KM is believed to be about 2 渭M. The enzyme concentration is 200 nM and the substrate concentrations range from 0.1 渭M to 10 渭M. What is wrong with this experimental setup and how could you fix it?

Short Answer

Expert verified

The problem can be fixed by reducing the concentration of enzyme.

Step by step solution

01

Rate equation

The rate equation for a single-substrate enzyme-catalyzed reactionis known as the Michaelis鈥揗enten equation. Through the Michaelis constant KM, a measure of substrate-binding affinity, this equation connects the starting reaction rate (v0), the maximal reaction rate (Vmax), and the initial substrate concentration [S].

02

Mistake in the experimental setup

The substrate curve for an enzyme with a KMof 2渭M is built as a velocity vs concentration plot. The enzyme concentration is 200nM, while the substrate concentration ranges from 0.1 to 10 micrograms per millilitre. The fundamental criterion for plotting this curve is that the enzyme concentration must be much lower than the substrate concentration, which is [E]<<[S].Reduce the enzyme concentration for each measurement of substrate concentration to solve the problem.

Thus, It has been fixed by reducing the concentration of the enzymefor each measurement of the substrate concentration.

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Most popular questions from this chapter

Ethanol in the body is oxidized to acetaldehyde (CH鈧僀HO) by liveralcohol dehydrogenase (LADH). Other alcohols are also oxidized byLADH. For example, methanol CH鈧僌H), which is mildly intoxicating, isoxidized by LADH to the quite toxic product formaldehyde (CH鈧侽). Thetoxic effects of ingesting methanol (a component of many commercialsolvents) can be reduced by administering ethanol. The ethanol acts as acompetitive inhibitor of the methanol by displacing it from LADH. Thisprovides sufficient time for the methanol to be harmlessly excreted bythe kidneys. If an individual has ingested 100 mL of methanol (a lethaldose), how much 100 proof whiskey (50% ethanol by volume) must beimbibe to reduce the activity of his LADH toward methanol to 5% of itsoriginal value? The adult human body contains -40 L of aqueous fluidsthroughout which ingested alcohols are rapidly and uniformly mixed.The densities of ethanol and methanol are both 0.79 g .cm-3. Assumethe KM values of LADH for ethanol and methanol to be 1.0 X 10鈦宦矼and 1.0 X 10鈦宦睲, respectively, and that KI = KM for ethanol.

If there is 10 渭mol of the radioactive isotope 鲁虏P (half-life 14 days) at t=0, how much will 鲁虏P remain at (a) 7 days, (b) 14 days, (c) 21 days,
and (d) 70 days?

Write the Lineweaver鈥揃urk (double reciprocal) equation and describe the features of a Lineweaver鈥揃urk plot.

You are trying to determine the KM for an enzyme. Due to a labmishap, you have only two usable data points:

Substrate concentration (渭M)

Reaction velocity (渭M s鈦宦�)

1

5

100

50

Use these data to calculate an approximate value for KM. Is this valuelikely to be an overestimate or an underestimate of the true value? Explain.

Is it necessary for measurements of reaction velocity to be expressed in units of concentration per time (M s鈦宦�, for example) to calculate an enzyme's KM?
See all solutions

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