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HomeHomework HelpbiochemistryEnzyme Inhibitors

Enzyme Inhibitors

Enzyme inhibitors are molecules that decrease enzyme activity; competitive inhibitors bind to the active site of the enzyme, preventing substrate binding, while noncompetitive inhibitors bind to an alternative site, altering the enzyme's function regardless of substrate presence.

intermediate
2 hours
Biochemistry
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Overview

Enzyme inhibitors play a crucial role in regulating biochemical reactions by decreasing enzyme activity. They can be classified into two main types: competitive and noncompetitive inhibitors. Competitive inhibitors compete with substrates for the active site, while noncompetitive inhibitors bind to ...

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Key Terms

Enzyme
A protein that accelerates chemical reactions.

Example: Amylase helps break down starch into sugars.

Inhibitor
A substance that decreases enzyme activity.

Example: Penicillin inhibits bacterial enzymes.

Active Site
The region on an enzyme where substrates bind.

Example: The active site of lactase binds lactose.

Substrate
The reactant molecule that an enzyme acts on.

Example: Glucose is a substrate for many enzymes.

Competitive Inhibition
Inhibition where the inhibitor competes with the substrate for the active site.

Example: Malonate competes with succinate in the enzyme succinate dehydrogenase.

Noncompetitive Inhibition
Inhibition where the inhibitor binds to an enzyme regardless of substrate presence.

Example: Lead can inhibit enzymes by binding to sites other than the active site.

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Key Concepts

Competitive InhibitionNoncompetitive InhibitionEnzyme ActivitySubstrate Concentration