Enzyme Inhibition quiz #1 Flashcards
Enzyme Inhibition quiz #1
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What is the difference between competitive and noncompetitive enzyme inhibitors?
Competitive inhibitors bind to the enzyme's active site, blocking substrate access, while noncompetitive inhibitors bind to an allosteric site, changing the enzyme's shape and preventing substrate binding. Why is enzyme inhibition important in biological systems?
Enzyme inhibition is important because it helps regulate the speed of chemical reactions in cells, maintaining metabolic balance and allowing for control over enzyme activity. How do competitive inhibitors affect enzyme activity?
Competitive inhibitors decrease enzyme activity by competing with the substrate for binding to the active site, thus preventing the substrate from binding and slowing down the reaction. How do noncompetitive inhibitors reduce the activity of an enzyme?
Noncompetitive inhibitors bind to an allosteric site on the enzyme, causing a change in the enzyme's shape that prevents the substrate from binding to the active site. What is the main function of enzyme inhibitors in cells?
Enzyme inhibitors slow down or stop enzyme activity to regulate the speed of chemical reactions in cells. How do competitive inhibitors interfere with enzyme activity?
Competitive inhibitors bind to the enzyme's active site, blocking the substrate from binding and thus slowing down the reaction. Where do noncompetitive inhibitors bind on an enzyme, and what is the result?
Noncompetitive inhibitors bind to an allosteric site, causing the enzyme to change shape and preventing the substrate from binding to the active site. Why is enzyme inhibition important for metabolic balance?
Enzyme inhibition helps control the rate of chemical reactions, ensuring that metabolic processes do not proceed too quickly or slowly, which maintains balance in the cell. What is the difference between competitive and noncompetitive enzyme inhibitors?
Competitive inhibitors bind to the active site and compete with the substrate, while noncompetitive inhibitors bind to an allosteric site and change the enzyme's shape. How does the binding of a noncompetitive inhibitor affect the enzyme's active site?
The binding of a noncompetitive inhibitor to the allosteric site alters the shape of the active site, preventing the substrate from binding and inhibiting catalysis.
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