Enzymes are protein molecules that act as a catalyst in biological reactions while inhibitors are low molecular weight chemical compounds that decrease the enzyme-catalyzed reactions. Enzyme inhibition can be defined as a science of enzyme-substrate activity influenced by the presence of an organic substance or inorganic metal or biosynthetic compound due to their covalent or non-covalent interactions with enzyme active site resulting in a decrease, reduction or termination of the enzyme activity during biological reaction.
Types of Inhibitors
Inhibitors can reduce activity by either reversible process where activity may be restored by the removal of the inhibitor by dilution or dialysis method. It can also be an irreversible process where the loss of activity is time dependent and cannot be recovered during the timescale of interest. They can modify one amino acid, or several side chain(s) required in enzyme catalytic activity. Heavy metal ions (e.g. mercury and lead) should generally be prevented from coming into contact enzymes as they usually cause such irreversible inhibition by binding strongly to the amino acid backbone.
Enzyme inhibition behavior and inhibitor structure-function relationship with enzyme active site clarify the mechanisms of actions and physiological regulation of metabolic enzymes. Some examples are: drug and toxin action, iodoacetamide deactivate Cys amino acid in an enzyme side chain e.t.c.
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