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Questions and Answers
What is the primary function of enzymes in biological systems?
What is the primary function of enzymes in biological systems?
- Providing structural support to cells
- Regulating body temperature
- Transporting genetic material
- Acting as catalysts for chemical reactions (correct)
Which of the following is true about most enzymes?
Which of the following is true about most enzymes?
- They are RNA molecules
- They are composed of nucleic acids
- They are involved in maintaining cell structure
- They are globular proteins (correct)
What is the purpose of enzyme inhibition?
What is the purpose of enzyme inhibition?
- To prevent enzyme catalysis (correct)
- To improve enzyme specificity
- To increase enzyme stability
- To accelerate enzymatic reactions
What is the key role of enzyme co-factors?
What is the key role of enzyme co-factors?
How do enzymes interact with their substrates?
How do enzymes interact with their substrates?
What do Michaelis-Menten and Lineweaver-Burk Plots describe?
What do Michaelis-Menten and Lineweaver-Burk Plots describe?
Which enzyme has the highest turnover number?
Which enzyme has the highest turnover number?
What type of inhibition occurs when the inhibitor binds with the enzyme at a site which is distinct from the substrate binding site?
What type of inhibition occurs when the inhibitor binds with the enzyme at a site which is distinct from the substrate binding site?
In which type of inhibition is there no change in the Vmax for the reaction?
In which type of inhibition is there no change in the Vmax for the reaction?
Which type of inhibition decreases both the apparent KM and Vmax for the reaction?
Which type of inhibition decreases both the apparent KM and Vmax for the reaction?
What is a measure of the affinity of an inhibitor drug for an enzyme?
What is a measure of the affinity of an inhibitor drug for an enzyme?
Which enzyme drug targets hypertension?
Which enzyme drug targets hypertension?
What is the main mechanism of action for statins in treating cardiovascular disease?
What is the main mechanism of action for statins in treating cardiovascular disease?
Which enzyme is targeted by NSAIDs like aspirin and ibuprofen?
Which enzyme is targeted by NSAIDs like aspirin and ibuprofen?
What happens to the Vmax for the reaction in non-competitive inhibition?
What happens to the Vmax for the reaction in non-competitive inhibition?
What is the suffix commonly added to the names of enzymes?
What is the suffix commonly added to the names of enzymes?
Which of the following is NOT a main class of enzymes based on the type of reaction they catalyze?
Which of the following is NOT a main class of enzymes based on the type of reaction they catalyze?
What is the function of a prosthetic group in relation to enzymes?
What is the function of a prosthetic group in relation to enzymes?
Which of the following is an example of a cofactor for enzymes?
Which of the following is an example of a cofactor for enzymes?
What is the name for the complete, catalytically active enzyme together with its bound cofactor and/or metal ion?
What is the name for the complete, catalytically active enzyme together with its bound cofactor and/or metal ion?
Which type of metabolic reactions involve the formation of bonds between molecules and require more energy than they produce?
Which type of metabolic reactions involve the formation of bonds between molecules and require more energy than they produce?
What role do enzymes play in cellular metabolic reactions?
What role do enzymes play in cellular metabolic reactions?
What is the main function of enzymes in metabolic reactions?
What is the main function of enzymes in metabolic reactions?
How do enzymes accelerate the rate of a reaction?
How do enzymes accelerate the rate of a reaction?
Which model of enzyme action involves a conformational change in the enzyme due to substrate binding?
Which model of enzyme action involves a conformational change in the enzyme due to substrate binding?
What factor affects enzyme function by altering the charges on the enzyme and substrate molecules?
What factor affects enzyme function by altering the charges on the enzyme and substrate molecules?
What is the effect of increasing enzyme concentration on reaction rate?
What is the effect of increasing enzyme concentration on reaction rate?
What happens to enzyme activity when the temperature exceeds the optimum level?
What happens to enzyme activity when the temperature exceeds the optimum level?
What is the main effect of increasing substrate concentration on reaction rate?
What is the main effect of increasing substrate concentration on reaction rate?
What is the pH range in which pepsin functions as a digestive enzyme?
What is the pH range in which pepsin functions as a digestive enzyme?
How does extreme pH affect enzymes?
How does extreme pH affect enzymes?
What disrupts the attraction between charged amino acids in enzymes?
What disrupts the attraction between charged amino acids in enzymes?
What is enzyme kinetics?
What is enzyme kinetics?
Who proposed the Michaelis-Menten Kinetics model?
Who proposed the Michaelis-Menten Kinetics model?
What is the 'saturation effect' exhibited by all enzymes with their substrates?
What is the 'saturation effect' exhibited by all enzymes with their substrates?
What determines the rate of formation of the enzyme-substrate complex in the Michaelis-Menten Kinetics model?
What determines the rate of formation of the enzyme-substrate complex in the Michaelis-Menten Kinetics model?
What does the Michaelis-Menten Equation (Vmax = [S][E]/KM) describe?
What does the Michaelis-Menten Equation (Vmax = [S][E]/KM) describe?
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Study Notes
- Pepsin and trypsin are two different digestive enzymes with extreme pH optima: pepsin functions in the stomach at pH 2-3, while trypsin operates in the small intestines at pH 8.
- Extreme pH levels can lead to enzyme denaturation, disrupting the attraction between charged amino acids and distorting the enzyme's 3D structure, resulting in loss of substrate fit.
- Enzymes are intolerant of extreme salinity, which disrupts attraction between charged amino acids, affects 2° and 3° enzyme structure, and ultimately disrupts bonds and the enzyme's 3D shape, leading to decreased reaction rate.
- Enzyme kinetics is the study of the rates of chemical reactions catalyzed by enzymes and provides insight into enzyme catalysis, their role in metabolism, the mechanisms of enzyme inhibition, and the mechanisms of metabolic control.
- In 1913, Michaelis and Menten proposed the Michaelis-Menten Kinetics model, which describes how enzymes increase the rate of metabolic reactions and how reaction rates depend on the concentration of enzyme and substrate.
- All enzymes exhibit a 'saturation effect' with their substrates, which means that at low substrate concentrations, the reaction rate is proportional to substrate concentration. However, as substrate concentration increases, the reaction rate no longer remains proportional and eventually becomes constant and independent of substrate concentration.
- Michaelis and Menten proposed a scheme for a saturating enzyme-catalyzed single substrate reaction, where the free enzyme binds its substrate to form an enzyme-substrate complex, which either undergoes further transformation to yield a final product or breaks down to reform the free enzyme and substrate.
- The rate of formation of the enzyme-substrate complex is determined by the rate constant, k1, while the rate of breakdown of the complex is determined by the rate constant, k-1, and the rate constant, k2.
- By applying the equilibrium constant equation and rearranging, the Michaelis-Menten equation (Vmax = [S][E]/KM) was derived, which describes the relationship between reaction velocity and substrate concentration.
- Michaelis and Menten derived the Michaelis-Menten Equation from the Michaelis-Menten Kinetics model.
- Michaelis-Menten Kinetics can be represented graphically using Lineweaver-Burk Plot and Eadie-Hofstee Plot for determining the kinetic parameters, including Vmax and KM.
- KM (Michaelis Constant) is a key parameter in Michaelis-Menten Kinetics, which has the same unit as the substrate, represents the substrate concentration at which the reaction velocity is 50% of the maximum velocity (Vmax), and indicates the enzyme's affinity for its substrate.
- KM values vary for different enzymes, with lower values indicating a higher affinity for the substrate, while higher values indicate a lower affinity for the substrate.
- Vmax is the maximum velocity or rate of reaction, giving an idea of how fast the reaction can occur under ideal circumstances and revealing the turnover number of an enzyme.
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