Enzyme Catalysis Quiz Questions

The active site of an enzyme binds the substrate of the reaction it catalyses more tightly than it does the transition state intermediate

The active site of an enzyme binds the substrate of the reaction it catalyses less tightly than it does the transition state intermediate.

The active site of an enzyme binds the product of the reaction it catalyses more tightly than it does the transition state intermediate.

The active site of an enzyme is complementary to the substrate of the reaction it catalyses

An enzyme cannot change the equilibrium position of the reaction it catalyses but it lowers the energy of activation of that reaction.

An enzyme can change the equilibrium position of the reaction it catalyses by lowering the energy of activation of that reaction.

An enzyme can lower the energy of activation of the reaction it catalyses by increasing the molecular collisions between the molecules.

An enzyme lowers the free energy difference between substrate(s) and product(s) but it cannot change the equilibrium position of the reaction it catalyses.

Km, the Michaelis constant, is defined as the concentration of substrate required for the reaction to reach maximum velocity.

Km, the Michaelis constant, is defined as the dissociation constant of the enzyme-substrate complex.

Km, the Michaelis constant, is a measure of the affinity the enzyme has for its substrate.

Km, the Michaelis constant, is expressed in terms of the reaction velocity.

A competitive inhibitor and substrate can bind simultaneously to the enzyme.

The Vmax and Km (Michaelis constant) for a reaction are unchanged in the presence of a competitive inhibitor.

The Km for a reaction remains unchanged in the presence of a competitive inhibitor.

The Vmax for a reaction remains unchanged in the presence of a competitive inhibitor.

Allosteric enzymes are typically single-subunit enzymes.

Allosteric enzymes show greater sensitivity to changes in substrate concentration compared to classical type enzymes with hyperbolic kinetics.

Allosteric enzymes show Michaelis-Menten kinetics.

Allosteric enzymes show reduced sensitivity to changes in substrate concentration compared to classical type enzymes with hyperbolic kinetics.

He rate of formation of the transition state intermediate determines the overall free energy change of the reaction.

The active site of an enzyme is perfectly complementary to the substrate in its ground state.

The rate of formation of the transition state intermediate determines the overall reaction rate.

Natural substrates bind to enzymes more tightly than transition state analogues

Competitive inhibition can be overcome by the addition of large amounts of substrate to a reaction.

The addition of large amounts of substrate to a reaction cannot overcome the effect of a competitive inhibitor.

A competitive inhibitor can bind to the enzyme-substrate complex.

The Vmax of a reaction decreases in the presence of a competitive inhibitor.

DNA gyrase

DNA polymerase

Carbonic unhydrase

Pepsin

Allosteric inhibition

Feedback inhibition

Competitive inhibition

Non-competitive inhibition

Succinic dehydrogenase by malonic acid

Cytochrome oxidase by cyanide

Hexokinase by glucose-6-phosphate

Carbonic anhydrase by carbon dioxide