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___ inhibitor would bind very tightly to an enzyme often forming a covalent bond with an amino acid residue at active site of the enzyme

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Final answer:

Irreversible inhibitors inactivate enzymes by covalently binding to a group at the active site. This type of inhibition is often irreversible, as the bonds between the inhibitor and enzyme are not easily broken.

Step-by-step explanation:

An irreversible inhibitor inactivates an enzyme by bonding covalently to a particular group at the active site. When the inhibitor is bound, the enzyme active site is blocked, the substrate does not bind, and catalysis cannot occur.

This type of inhibition is often irreversible because the bonds between the inhibitor and the enzyme are not easily broken.

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User Chandan Y S
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