(a) An experiment can be designed to test the effect of different temperature levels on the functioning of catalase. Identify the appropriate independent and dependent variables for this experiment. (b) Identify an appropriate method to measure the dependent variable in this experiment and justify your choice.
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- Based on this information, what type of enzyme would ornithine decarboxylase be? I searched it up on Google and sources say it is a lyase because it catalyzes cleavage without H2O, but in equation 1, isn't water part of the reaction? Is decarboxylase still a lyase because water is a reactant, not a catalyst?Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?When a mixture of 3-phosphoglycerate and 2-phosphoglycerate is incubated at 25°C in the presence of the enzyme phosphoglycerate mutase (which catalyzes the intervconversion of the two substances) until equilibrium is reached, the final mixture contains 6 times as much 2-phosphoglycerate as 3-phosphoglycerate. Which of the following statements is most nearly correct when applied to the reaction shown below: 3-phosphoglycerate ------> 2-phosphoglycerate (R=8.315 J/mole.K) A. △G°' = +12.7 kJ/mole B. △G°' = 0 C. △G°' is incalculably large and positive D. △G°' = -4.44 kJ/mole E. △G°' cannot be calculated from the information gven
- Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneousThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…Hexokinase is an important enzyme in the metabolism of glucose. If theconcentration of hexokinase in our eukaryotic cell is 20 μM, how many glucose molecules are present per hexokinase molecule?
- Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?In covalent catalysis, either nucleophilic catalysis or electrophilic catalysis occurs. Do you agree or disagree with this statement? Explain.You have the following pathway: If an isolated liver cell runs out of glucose, the cell will break down glycogen into Glucose-1-Phosphate (Glucose-1-P). The isolated liver cell will then use the enzyme phosphoglucomutase to convert Glucose-1-P to Glucose-6-P, which can enter glycolysis. If you remove all glucose and add a drug that inhibits phosphoglucomutase, which molecule will most likely accumulate in this system? A. Glucose B. Glucose 1 phosphate C. Glucose 6 phosphate D. Lactate E. CO2
- The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.