BIOLOGY
ENZYMES
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Question
[CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
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The inhibitor molecule causes the enzyme to be denatured so the substrate cannot bind to it.
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The inhibitor molecule binds to side chains on the polypeptide chain of the enzyme so it cannot interact with its substrate.
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The inhibitor molecule competes with the substrate to bind with active site
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None of the above
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Detailed explanation-1: -A substance that permanently blocks the action of an enzyme. In cancer treatment, irreversible enzyme inhibitors may block certain enzymes that cancer cells need to grow and may kill cancer cells. They are being studied in the treatment of some types of cancer.
Detailed explanation-2: -The noncompetitive inhibitor binds to a different site on the enzyme; it doesn’t block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently.
Detailed explanation-3: -An irreversible inhibitor will bind to an enzyme so that no other enzyme-substrate complexes can form. It will bind to the enzyme using a covalent bond at the active site which therefore makes the enzyme denatured.
Detailed explanation-4: -An irreversible inhibitor inactivates an enzyme by bonding covalently to a particular group at the active site. The inhibitor-enzyme bond is so strong that the inhibition cannot be reversed by the addition of excess substrate.