Exploring Enzymes and Their Functions

What is the primary structure of an enzyme?

• The active site of the enzyme.

• The cofactor required for enzyme activity.

• The unique sequence of amino acids.

• The three-dimensional shape of the enzyme.

How does the active site of an enzyme facilitate catalysis?

• The active site increases activation energy and destabilizes the transition state.

• The active site binds substrates without altering their energy levels.

• The active site lowers activation energy and stabilizes the transition state.

• The active site prevents substrate binding to the enzyme.

What role do coenzymes play in enzyme activity?

• Coenzymes are structural components of enzymes.

• Coenzymes enhance enzyme activity by acting as essential cofactors that assist in the catalytic process.

• Coenzymes are waste products of enzyme reactions.

• Coenzymes inhibit enzyme activity by blocking active sites.

Differentiate between cofactors and coenzymes with examples.

• Cofactors are always organic molecules, while coenzymes are inorganic.

• Cofactors are enzymes that speed up reactions, while coenzymes are substrates.

• Cofactors and coenzymes are the same and can be used interchangeably.

• Cofactors are non-protein molecules (e.g., metal ions like Zn²⁺), while coenzymes are organic cofactors (e.g., NAD⁺, derived from niacin).

Explain how temperature affects enzyme activity.

• Enzymes are only active at low temperatures.

• Temperature affects enzyme activity by increasing it up to a certain point, after which high temperatures can denature the enzyme and reduce activity.

• Higher temperatures always increase enzyme activity.

• Temperature has no effect on enzyme activity.

What is enzyme inhibition and how does it occur?

• Enzyme inhibition is the process by which a molecule decreases the activity of an enzyme.

• Enzyme inhibition increases the activity of an enzyme.

• Enzyme inhibition is the process of enzyme synthesis.

• Enzyme inhibition occurs only in the presence of heat.

Describe the allosteric regulation of enzymes.

• Allosteric regulation involves the direct binding of substrates to the active site.

• Allosteric regulation is the process of enzyme degradation by heat.

• Allosteric regulation of enzymes is the modulation of enzyme activity through the binding of molecules at sites other than the active site, resulting in conformational changes.

• Allosteric regulation refers to the irreversible modification of enzyme structure.

How do competitive and non-competitive inhibitors differ?

• Competitive inhibitors affect substrate binding; non-competitive inhibitors affect enzyme activity.

• Competitive inhibitors affect enzyme structure; non-competitive inhibitors affect substrate concentration.

• Competitive inhibitors increase enzyme activity; non-competitive inhibitors decrease substrate binding.

• Both competitive and non-competitive inhibitors bind to the active site of the enzyme.

What is the significance of enzyme specificity?

• Enzyme specificity is significant because it allows for precise control of biochemical reactions, ensuring efficiency and regulation in metabolic pathways.

• Enzyme specificity is only important in industrial applications.

• Enzyme specificity increases the number of reactions that can occur simultaneously.

• Enzyme specificity is irrelevant to metabolic pathways.

How do pH levels influence enzyme function?

• Enzymes are only influenced by temperature, not pH.

• All enzymes function best at a neutral pH of 7.

• pH levels influence enzyme function by affecting their structure and activity, with each enzyme having an optimal pH range.

• pH levels have no effect on enzyme function.