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Ch. 8 - Energy and Enzymes: An Introduction to Metabolism

Chapter 8, Problem 5

Explain the lock-and-key model of enzyme activity. What is incorrect about this model?

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Hi everyone. Let's look at our next question. It says identify the model for enzyme substrate interaction. That suggests that the enzyme and the substrate have complementary geometric shapes that fit exactly into one another. So, let's look at our answer choices. We'll notice that we've got three different model choices and then Choice C. Says both A and B. So there's a possibility that more than one could be correct. So, again, the key word here is exactly we wanna imagine sort of like our um our substrate and our enzyme fit together. Here's your substrate, here's your little enzyme and it's got this shape that fits exactly with the substrate. Well, that kind of model, as you can imagine, is called the lock and key model. Just as a key fits exactly into a lock. We have the substrate fitting exactly into the active side of the enzyme. So that is the name of the model that we're looking for. But let's just look at our other two model choices and see why they're not the correct answer here. Choice A says the induced fit model. Well, the induced fit model imagines that um here's our substrate, here's our enzyme and it's got an active site that's not quite the right shape for this. So this binds anyway. But then after binding. So this we have it's it's settled in there but not really fitting exactly. We see a confirmation all change in the enzyme where the active site changes shape to fit the substrate more exactly after binding. So we don't have this exact fit in the induced fit model. Instead, we have a change to the active site of the enzyme. So that's why induced fit is not the correct answer here. And that's also why we wouldn't choose choice C. Because A is not correct. And finally, we have the confirmation selection model that's kind of the reverse idea of the induced fit. That says that we have um I'm sorry, not the reverse idea, but it's it's sort of like induced fit but a little different. It involves here's our enzyme with its active site, here's our substrate. Just put a little box here. So we don't get mixed up and they're not an exact fit. But then prior to their binding this enzyme undergoes a conformational change that then changes the active site so that it combined. And the final step then, is this binding of the substrate into the active site that now fits it. But again, we don't have a perfect fit in the beginning. As with the lock and key model, we have a change to the active site immediately prior to the substrate binding with the active site that's called the confirmation selection model. So that's why that is not the correct answer here. We have sort of this this idea, this rigid lock and key model where the two fit together exactly. So which one um reflects that fitting exactly into one another. Again, that's choice B lock and key model. See you in the next video
Related Practice
Textbook Question

How does pH affect enzyme-catalyzed reactions? a. Protons serve as substrates for most reactions. b. Energy stored in protons is used to drive endergonic reactions. c. Proton concentration increases the kinetic energy of the reactants, enabling them to reach their transition state. d. The concentration of protons affects an enzyme's folded structure and reactivity.

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Textbook Question

What factors determine whether a chemical reaction is spontaneous or not?

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Textbook Question

Which of the following correctly describe an active site? Select True or False for each statement. T/F It is the location in an enzyme where substrates bind. T/F It is the place where a molecule or ion binds to an inactive enzyme to induce a shape change to make it active. T/F It is the portion of an enzyme where chaperones bind to help enzymes fold. T/F It is the site on an enzyme where catalysis occurs.

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Textbook Question

If you were to expose glucose to oxygen on your lab bench, why would you not expect to see it burn as described by the reaction in Figure 8.6? a. The reaction is endergonic and requires an input of energy. b.The reaction is not spontaneous unless an enzyme is added. c. The sugar must first be phosphorylated to increase its potential energy. d. Activation energy is required for the sugar and oxygen to reach their transition state.

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Textbook Question

In Figure 8.10, the energetic coupling of substrate phosphorylation and an endergonic reaction are shown. If the hydrolysis of ATP releases 7.3 kcal of free energy, use the graph in this figure to estimate what you would expect the ∆G values to be for the uncoupled reaction and the two steps in the coupled reaction.

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Textbook Question

You have discovered an enzyme that appears to function only when a particular sugar accumulates. Which of the following scenarios would you predict to be responsible for activating this enzyme? a. The sugar cleaves the enzyme to form the active conformation. b. The sugar is an allosteric regulatory molecule for the enzyme. c. The sugar is a competitive inhibitor for the enzyme. d. The sugar phosphorylates the enzyme to form the active conformation

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