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Ch.19 Enzymes and Vitamins
All textbooksMcMurry 8th EditionCh.19 Enzymes and VitaminsProblem 19.59
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Chapter 19, Problem 19.59

What kind of inhibition (uncompetitive, competitive, or irreversible) is present in each of the following:


a. Penicillin is used to treat certain bacterial infections. Penicillin is effective because it binds to the enzyme glycopeptide transpeptidase and does not dissociate.

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Identify the type of enzyme inhibition by understanding how penicillin interacts with the enzyme glycopeptide transpeptidase.
Recognize that penicillin binds to the enzyme and does not dissociate, indicating a permanent or long-lasting interaction.
Recall that irreversible inhibitors form a covalent bond with the enzyme, leading to permanent inactivation.
Consider that competitive inhibitors bind reversibly to the active site, and uncompetitive inhibitors bind to the enzyme-substrate complex, both of which are not applicable here.
Conclude that the type of inhibition where the inhibitor binds permanently and does not dissociate is known as irreversible inhibition.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Enzyme Inhibition

Enzyme inhibition refers to the process by which a molecule (inhibitor) decreases the activity of an enzyme. This can occur through various mechanisms, including competitive, uncompetitive, and irreversible inhibition, each affecting the enzyme's function differently. Understanding these types is crucial for analyzing how drugs like penicillin interact with bacterial enzymes.
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Enzyme Inhibition Concept 1

Irreversible Inhibition

Irreversible inhibition occurs when an inhibitor permanently binds to an enzyme, often through covalent bonds, leading to a long-lasting decrease in enzyme activity. In the case of penicillin, it binds to glycopeptide transpeptidase and forms a stable complex, effectively disabling the enzyme and preventing bacterial cell wall synthesis.
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Enzyme Inhibition Concept 1

Glycopeptide Transpeptidase

Glycopeptide transpeptidase is an essential enzyme in bacteria that catalyzes the cross-linking of peptidoglycan layers in the bacterial cell wall. By inhibiting this enzyme, penicillin disrupts cell wall integrity, leading to bacterial lysis and death. Understanding its role helps clarify how antibiotics target specific bacterial processes.
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Textbook Question

What general effects would you expect the following changes to have on the rate of an enzyme-catalyzed reaction for an enzyme that has its maximum activity at body temperature (about 37°C)?


c. Adding an organic solvent, such as methanol

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Textbook Question

What general effects would you expect the following changes to have on the rate of an enzyme-catalyzed reaction for an enzyme that has its maximum activity at body temperature (about 37°C)?


c. Adding an oxidizing agent, such as hydrogen peroxide

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Textbook Question

The text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.


b. What kinds of bonds are formed between an enzyme and each of these three kinds of inhibitors?

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Textbook Question

What kind of inhibition (uncompetitive, competitive, or irreversible) is present in each of the following:


c. The antibiotic deoxycycline inhibits the bacterial enzyme collagenase, slowing bacterial growth. Deoxycycline does not fit into the active site of collagenase and binds elsewhere on the enzyme.

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One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.

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The meat tenderizer used in cooking is primarily papain, a protease enzyme isolated from the fruit of the papaya tree. Why do you suppose papain is so effective at tenderizing meat?

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