Practice Questions

10. During medical treatment, several drugs produce their therapeutic effects by

A. Inhibiting specific enzymes involved in disease processes
B. Increasing the temperature of body tissues
C. Converting enzymes into hormones
D. Destroying all cellular proteins

Many medicines work by selectively inhibiting enzymes. Examples include drugs that inhibit bacterial enzymes or enzymes involved in cholesterol synthesis. The remaining options are biologically incorrect. Concept tested: Medical application of enzyme inhibitors.

nmdcat.online BIO NMDCAT
Jul 13, 2026

9. Concerning enzyme inhibition, the characteristic feature of non-competitive inhibitors is

A. Reduction in maximum enzyme activity
B. Complete prevention of substrate binding
C. Conversion of substrate into inhibitor
D. Increase in enzyme concentration

Non-competitive inhibitors decrease the maximum reaction rate because some enzyme molecules become inactive regardless of substrate concentration. The other statements are incorrect. Concept tested: Effect on enzyme kinetics.

nmdcat.online BIO NMDCAT
Jul 13, 2026

8. During an investigation, two reaction mixtures contain equal amounts of enzyme. Only one contains a competitive inhibitor. The mixture showing the greater increase in reaction rate after adding excess substrate is

A. The mixture containing the competitive inhibitor
B. The mixture without enzyme
C. The mixture containing a non-competitive inhibitor
D. The mixture containing irreversible inhibitor

Excess substrate successfully competes with a competitive inhibitor, increasing enzyme activity. This effect is not observed with non-competitive or irreversible inhibitors. Concept tested: Experimental reasoning.

nmdcat.online BIO NMDCAT
Jul 13, 2026

7. The biological significance of enzyme inhibitors includes

A. Regulation of metabolic pathways
B. Permanent synthesis of new enzymes
C. Continuous activation of all enzymes
D. Elimination of cofactors from cells

Many enzyme inhibitors regulate metabolic pathways by controlling enzyme activity. The other options do not represent normal biological roles of inhibitors. Concept tested: Physiological importance of inhibitors.

nmdcat.online BIO NMDCAT
Jul 13, 2026

6. During metabolism, heavy metal ions commonly reduce enzyme activity by

A. Binding to sulfhydryl groups and altering enzyme structure
B. Increasing substrate concentration
C. Acting as enzyme cofactors
D. Converting enzymes into products

Heavy metals such as mercury and lead bind to sulfhydryl (-SH) groups, distorting enzyme structure and causing irreversible inhibition. The remaining options are incorrect mechanisms. Concept tested: Heavy metal inhibition.

nmdcat.online BIO NMDCAT
Jul 13, 2026

5. Among the following statements, the effect of irreversible inhibitors is best described as

A. Permanent loss of enzyme activity
B. Temporary occupation of the active site
C. Increased substrate affinity
D. Formation of additional enzyme molecules

Irreversible inhibitors form stable covalent or very strong bonds with enzymes, permanently inactivating them. Other options are inconsistent with irreversible inhibition. Concept tested: Irreversible inhibition.

nmdcat.online BIO NMDCAT
Jul 13, 2026

4. The experimental observation indicates that enzyme activity remains low despite a marked increase in substrate concentration. The most appropriate explanation is

A. Non-competitive inhibition
B. Competitive inhibition
C. Substrate activation
D. Product acting as substrate

Since increasing substrate fails to restore activity, the inhibitor likely binds outside the active site and changes enzyme conformation. Competitive inhibition would be overcome by excess substrate. Concept tested: Interpretation of experimental data.

nmdcat.online BIO NMDCAT
Jul 13, 2026

3. Concerning non-competitive inhibition, the inhibitor primarily binds to

A. An allosteric site different from the active site
B. The substrate molecule
C. The enzyme-substrate complex only
D. The catalytic amino acid permanently

Non-competitive inhibitors bind at an allosteric site, altering enzyme shape and reducing activity regardless of substrate concentration. Other options do not correctly describe this inhibition. Concept tested: Allosteric regulation.

nmdcat.online BIO NMDCAT
Jul 13, 2026

2. During enzyme-catalyzed reactions, an increase in substrate concentration can reverse inhibition produced by

A. Competitive inhibitors
B. Non-competitive inhibitors
C. Irreversible inhibitors
D. Heavy metal poisoning

Competitive inhibition is reversible because substrate molecules can outcompete the inhibitor at high concentrations. Non-competitive and irreversible inhibitors cannot be overcome this way. Concept tested: Effect of substrate concentration on inhibition.

nmdcat.online BIO NMDCAT
Jul 13, 2026

1. Regarding enzyme inhibitors, the primary characteristic of a competitive inhibitor is

A. Binding to the active site of the enzyme
B. Binding permanently to the enzyme
C. Destroying the enzyme protein
D. Converting the enzyme into a substrate

Competitive inhibitors resemble the substrate and compete for the enzyme's active site. Increasing substrate concentration can overcome their effect. The other options describe irreversible inhibition or incorrect mechanisms. Concept tested: Competitive inhibition.

nmdcat.online BIO NMDCAT
Jul 13, 2026
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