Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product C. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
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- An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %Which of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
- Which of the following statements is true about effect of substrate concentration on enzyme activity ? The rate of reaction increases as the substrate concentration increases up to certain limit at which the reaction rate is maximal (Vmax.) At Vmax, the enzyme is completely saturated with the substrate, At Vmax, any increase in substrate concentration don't affect the reaction rate. All of themConsider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released EnergyThe figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?
- The change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the table below. Determine the Vmax and Km of the enzyme in the absence and presence of C. Is C an inhibitor or an activator of enzyme A? Determine the type of inhibition or activation. Rate of formation of Product B in the presence of 25 mg/mL C (mM/min) Substrate Rate of formation of (mM) Product B (mM/min) 0.5 21.5 14.1 1 30.2 22.2 1.5 34.9 27.0 2.5 39.8 33.1 3.5 42.0 36.3Which of the following statements are true about the relationships of [S], KM, and Vmax? (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
- Which of the following statements about Km is false? The km for a substrate will vary depending on the conditions of the reaction The km is equal to ½ vmax The kcat of a reaction will vary as it is equal to Vmax/km Km reflects the stability of the enzyme-substrate complex Both B and C are false Both A and C are false Not sure if 5 or 6 is correctAn experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results obtained are summarized in the table below. In all the experiments, the concentration of the enzyme is the same. Substrate Concentration Velocity (pmol/min) (pmol) 1.5 0.21 3 0.28 4 0.32 0.36 8 0.4 15 0.45 18 0.47 1. Plot or graph these results using the Lineweaver-Burk method. 2. Determine the KM and Vmax values. Show all equations and calculations.I Shown below is a plot of the rate of enzyme reaction to substrate concentration, where a substrate S binds reversibly to enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and regenerate the free enzyme E. E+S ES →E+ P For many enzymes, the rate of the reaction increases with substrate concentration, till it reaches a plateau, Vmax because the enzyme is sàturated, or all enzyme molecules are bound to substrate molecules. This is shown below in the graph as curve A. The substrate concentration that gives you a rate that is halfway to Vmax is called the Km, and is a useful measure of how quickly reaction rate increases with substrate concentration. a. Which of the curves B or C Vmax best demonstrates enzyme B. activity in the presence of a competitive inhibitor? Explain briefly why. 1/2 Vmax Vmax -- C b. Which of the curves B or C best demonstrates enzyme 1/2 Vmax activity in the presence of a noncompetitive inhibitor? Explain…