PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme concentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) Uninhibited With 1 mmol I-A With 1 mmol I-B 50 20 10 0.684 1.08 1.43 1.02 0.798 0.657 0.549 0.653 0.468 0.363 1.01 3.3 2.5 2.0 0.649 0.476 0.374 0.311 0.296 0.250 Comment on these results.
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- Question: Determine the Km and Vmax for this enzyme/substrate combination. [Substrate] (mM) V0 (mM/min) 0.25 0.183 0.50 0.356 1.00 0.665 2.50 1.45 5.00 2.35 What is the concentration of substrate necessary to achieve a turnover rate of 1.00 mM/min?Problem 3. Excess alcohol consumption can result in fatty liver disease. Liver cells synthesize triacylglycerides from fatty acids formed by fatty acid synthesis. Excess triacylglycerides can accumulate in the liver compromising normal liver function. D.Explain how stimulation of the rate of fatty acid synthesis changes the rate of fatty acid oxidation based on allosteric regulation of the rate-limiting step of beta-oxidation.Problem 2. When alcohol is consumed in excessive quantities, the resulting levels of NADH cause metabolic abnormalities, and one of which is high levels of fatty acid synthesis. Fatty acid synthesis, also a cytoplasmic process, uses acetyl-CoA as a substrate and NADPH as a reducing agent. Based on the above, we can see how acetate is converted to acetyl-CoA in the mitochondria, but fatty acid synthesis takes place in the cytosol. Complete the analysis by accounting for high acetyl-CoA concentration in the cytosol. Study the summary of reactions of citrate metabolism. E. How would increasing the rate of the reaction catalyzed by malate dehydrogenase decrease the concentration of oxaloacetic acid (OAA) in the cytosol? F. How would decreasing the concentration of OAA increase the concentration of acetyl-CoA in the cytosol by Le Chatelier’s principle?
- Velocity (mmol/minute) [S], (mM) No inhibitor Inhibitor 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8 The kinetics of an enzyme are measured as a function of substrate in the presence and the in absence of 2mM inhibitor (I). What are the values of Vmax and KM in the absence of inhibitor? In its presence? In its presence? What is the type of inhibition?Problem # 3: Calculate the number of moles of ATP produced from the complete oxidation of 900 g glucose in the cells. Show your computation/solution.Q14. The characterization of an enzyme by measuring the rate of its reaction includes determining the values for both Vmax and Km. Which of the following statements about these two parameters is correct? A. The presence of a competitive inhibitor will result in a lower Vmax. B. The Km increases as enzyme-substrate affinity increases. C. A reaction that has a high Vmax may have a low Km. D. An increase in enzyme concentration will only affect the Km not the Vmax.
- An enzyme has a KM = 10 mM and Vmax = 100 mmol/min. Identify the substrate concentration (in mM) in which the velocity will near Vmax when there is a 10-fold decrease in KM.Problem 1: For your new year's resolution, you resolve to lose 5lbs of body fat through physical exercise. If you work out hard, you can generate 200 W of mechanical power and be 20% efficient at it. How long will you have to exercise at this rate to burn the desired amount of fat? If you chose to diet instead and cut your food intake of 2400 kcal/day to 1600 kcal/day, how long will it take you to lose the desired amount of weight?Problem 3. Excess alcohol consumption can result in fatty liver disease. Liver cells synthesize triacylglycerides from fatty acids formed by fatty acid synthesis. Excess triacylglycerides can accumulate in the liver compromising normal liver function. A.Explain how palmitoyl-CoA is related to fatty acyl CoASH esters (acyl-CoA) B.Explain how increasing the rate of triglyceride formation changes the concentration of acyl-CoA in the cytosol. C.Explain how the rate of triglyceride formation stimulates the rate of fatty acid synthesis based on the concentration of palmitoyl-CoA in the cytosol
- 22. What is a major benefit of calculating catalytic efficiencies? Group of answer choices It determines whether a catalytic reaction is cooperative It allows you to compare different substrate preferences for an enzyme It tells you the rate of an enzyme reaction It allows you to determine the efficiency of the enzyme being studied9:34 AM You sent Help me with this one Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…Q14. The transition state is an important intermediate that can influence the rate of an exergonic reaction. Which of the following statements about the transition state is correct? A. At the transition state reacting molecules are the most stable. B. The more molecules that can reach the transition state the faster the reaction will be. C. The transition state increases in the presence of an enzyme. D. If the transition state is high enough the reaction can move from being exergonic to being endergonic.