Multiple Choice
Which of the following represents a reactant or input for the light reaction of photosynthesis?
3. Acids and Bases
Organic Chemistry Reactions
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In the context of organic chemistry reactions, how does an allosteric inhibitor affect enzyme activity?
A
It increases the enzyme's affinity for the substrate, enhancing reaction rate.
B
It binds to the active site of the enzyme, preventing substrate binding.
C
It binds to a site other than the active site, causing a conformational change that reduces enzyme activity.
D
It competes with the substrate for the active site, directly blocking substrate access.
Verified step by step guidance1
Understand the role of enzymes in organic chemistry: Enzymes are biological catalysts that speed up chemical reactions by lowering the activation energy required for the reaction to proceed.
Define allosteric inhibition: An allosteric inhibitor is a molecule that binds to an enzyme at a site other than the active site, known as the allosteric site.
Explain the effect of allosteric binding: When an allosteric inhibitor binds to the allosteric site, it induces a conformational change in the enzyme's structure.
Discuss the impact on enzyme activity: This conformational change can reduce the enzyme's activity by altering the shape of the active site, making it less effective at binding to the substrate.
Clarify the difference from competitive inhibition: Unlike competitive inhibitors, which bind to the active site and directly block substrate access, allosteric inhibitors do not compete with the substrate for the active site.
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