Understanding Enzyme Functions

What are the main types of enzymes?

• Proteases

• Carboxylases

• Phosphatases

• Hydrolases, Oxidoreductases, Transferases, Lyases, Isomerases, Ligases

Define the term 'enzyme kinetics'.

• Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions.

• Enzyme kinetics is the analysis of enzyme inhibitors.

• Enzyme kinetics refers to the measurement of enzyme concentrations.

• Enzyme kinetics is the study of protein structures.

What is the significance of the Michaelis-Menten equation?

• It is used to calculate the speed of light.

• The significance of the Michaelis-Menten equation lies in its ability to model enzyme kinetics and predict reaction rates.

• It explains the process of photosynthesis.

• It describes the structure of DNA.

List three factors that affect enzyme activity.

• Oxygen levels

• Presence of inhibitors

• Temperature, pH, substrate concentration

• Enzyme concentration

How does temperature influence enzyme function?

• Temperature influences enzyme function by increasing activity up to an optimal point, beyond which enzymes may denature.

• Enzymes function best at extremely high temperatures.

• Higher temperatures always increase enzyme stability.

• Temperature has no effect on enzyme activity.

What role does pH play in enzyme activity?

• pH has no effect on enzyme activity.

• pH changes do not influence substrate binding.

• pH affects enzyme activity by influencing the enzyme's structure and the charge of its active site, impacting substrate binding and reaction rates.

• Enzymes are only active at neutral pH levels.

Differentiate between competitive and non-competitive inhibitors.

• Competitive inhibitors increase the reaction rate by binding to the active site.

• Non-competitive inhibitors only affect substrate binding without altering enzyme structure.

• Competitive inhibitors permanently deactivate the enzyme by binding irreversibly.

• Competitive inhibitors compete with the substrate for the active site, while non-competitive inhibitors bind to a different site and reduce enzyme activity without competing for the active site.

What are coenzymes and how do they function?

• Coenzymes are organic molecules that assist enzymes in biochemical reactions by acting as carriers for chemical groups or electrons.

• Coenzymes are waste products generated during metabolic processes.

• Coenzymes are proteins that directly catalyze biochemical reactions.

• Coenzymes are inorganic substances that inhibit enzyme activity.

Explain the role of cofactors in enzyme activity.

• Cofactors are waste products of enzyme reactions.

• Cofactors enhance enzyme activity by assisting in substrate binding and participating in the reaction.

• Cofactors inhibit enzyme activity by blocking substrate access.

• Cofactors are only necessary for non-protein enzymes.

What is an allosteric site on an enzyme?

• A permanent binding site that changes the enzyme's structure.

• A location where inhibitors can only bind irreversibly.

• An allosteric site is a regulatory site on an enzyme where molecules can bind, influencing enzyme activity.

• A site where substrates bind to initiate a reaction.