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In drug-enzyme interactions, a competitive inhibitor binds to the enzyme's active site and competes with the substrate for that site — this makes option (4) a correct statement. A non-competitive inhibitor binds to the allosteric site (a site other than the active site), which makes option (1) correct. When an allosteric inhibitor binds to the allosteric site, it induces a conformational change in the enzyme that alters the shape of the active site, preventing the substrate from binding effectively — this makes option (2) correct.
Option (3) states that an allosteric inhibitor competes with the enzyme's active site. This is wrong because an allosteric inhibitor, by definition, binds at a site different from the active site. It does not compete with the substrate for the active site; instead, it inhibits the enzyme by changing the conformation of the active site from a remote location. Competition with the active site is the hallmark of competitive inhibition, not allosteric inhibition.
The wrong statement is therefore option (3).
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