ENZYMES

Enzyme activity is not enhanced by inhibitors; inhibitors reduce enzyme activity.

Enzymes are primarily composed of proteins.

Metabolic reactions include both constructive (anabolic) and destructive (catabolic) reactions.

The point where the enzyme is most active is known as the optimum pH.

The induced fit model suggests that the active site continuously changes its shape until the substrate binds to it.

Proteases act on proteins, not carbohydrates.

Chemical reactions require proper temperature and pressure conditions to carry out at a proper rate.

Organic solvents are not typically considered a factor affecting enzyme activity.

The rate of reaction generally increases with an increase in temperature.

The lock and key model suggests that the enzyme and substrate possess specific complementary geometric shapes.

Enzymes speed up chemical reactions by reducing the activation energy.

The nature of end products remains unaffected by the presence of enzymes in a reaction.

Constructive metabolic reactions (anabolism) involve the formation of large molecules.

Activators can boost enzyme activity.

The region on an enzyme where the substrate binds is called the active site.

Inhibitors reduce or block enzyme activity.

Enzyme reaction rates initially increase with an increase in temperature.

Enzymes lose their structure and function due to extreme changes in pH.

Anabolism is considered a "constructive" metabolic reaction.

The minimum energy required to initiate a chemical reaction is termed activation energy.

Enzymes reduce the activation energy needed for biochemical reactions.

Enzymes are primarily composed of proteins.

The specific region on an enzyme where a substrate binds is called the active site.

Enzymes are highly sensitive to pH, temperature, and substrate concentration.

Activators can enhance the activity of an enzyme.

The temporary structure formed when an enzyme binds to its substrate is called the enzyme-substrate complex.

The Induced Fit model suggests that the enzyme's active site adjusts its shape to fit the substrate.

The two primary types of metabolic reactions are anabolism and catabolism.

Initially, 2 ATP are required to break down a glucose molecule.

Catabolism involves breaking down large molecules into smaller ones.

Enzymes speed up the rate of biochemical reactions.

The term for the reactant in an enzyme-catalyzed reaction is substrate.

The active site of an enzyme is complementary in shape to the substrate.

Enzyme specificity means that one enzyme catalyzes one reaction or related reactions.

NAD is an example of an organic cofactor.

A prosthetic group is a tightly bound organic cofactor.

Enzyme inhibitors reduce activity by binding to the enzyme and blocking its function.

At substrate saturation, increasing substrate concentration has no effect on the reaction rate.

The optimum temperature for human enzymes is approximately \( 37^{\circ} \text{C} \).

High temperatures reduce enzyme activity because they break bonds and denature the enzyme.

Pepsin functions best in an acidic pH environment.

Emil Fischer proposed the "Lock and Key" model of enzyme action.

The Lock and Key model fails to explain the stabilization of the transition state.

The Induced Fit model suggests that the enzyme's active site is flexible and shape-adjusting.

The Induced Fit model explains that the enzyme’s active site changes shape during substrate binding.

The Lock and Key model compares the enzyme-substrate interaction to a key fitting into a lock.

Daniel Koshland’s model addresses a limitation of the Lock and Key theory related to active site flexibility.

The specificity of an enzyme for its substrate is primarily determined by the active site’s geometric shape and amino acid properties.

Pepsin is an example of an extracellular enzyme.

Lipase specifically acts on ester bonds in lipids/fats.

ATPase is classified as an intracellular enzyme.

Proteases exclusively catalyze reactions involving proteins.