Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme pes
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- Which of the following is TRUE concerning the induced fit model of enzyme catalysis? * (One correct answer only) A. The active site can be influenced by molecules binding elsewhere on an enzyme B. The initial binding of enzyme and substrate is the most tightly bound conformation C. The induced fit must occur prior to the initial binding of enzyme and substrate in order for the reaction to proceed D. The binding of enzyme and substrate is weakest in the transition stateWhich of the following is NOT true? a. For many enzymes, Vmax is essentially equal to k3. b. Km is the reaction rate at 1/2 Vmax. c. At steady state the formation of ES is equal to the breakdown of ES. d. A Lineweaver-Burke plot generates a straight line. e. An Eadie-Hofstee plot generates a straight line.Which of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.
- Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…Which of the following statements is/are true about enzyme-catalyzed reactions? A. The reaction is faster than the same reaction. B. The free energy change of the reaction is opposite from the reaction in the absence of the enzymes. C. The reaction always goes in the direction toward chemical equilibrium. D. A and B only E. A, B and C
- The graph shows the reaction coordinate of an enzymatic reaction of substrate to product a) which number correlates with the overall Keq of the reaction going from S to P? b) which number correlates with the velocity of the reaction WITHOUT enzyme (ie. starting with only substrate)? C) which number correlates with the overall velocity of the reaction WITH SATURATED enzyme D) the initial velocity of this reaction increases by a specific factor in the presence of enzyme. The difference between which two numbers best correlates with this enhancement in velocity? 1) 3 and 1 2) 3and 2 3) 3 and 4 4) 3 and 5 5) 3 and 6In competitive inhibition, increasing concentrations of the inhibitor will have the following effect on the kinetics of the enzyme: A. Km will decrease. B. Vmax will stay the same. C. The reaction will cease because the inhibitor binds irreversibly. D. Km / Vmax will stay the same.The enzyme glutamine synthetase catalyzes the following reaction: glutamate + ATP + NH3 → glutamine + ADP + phosphate Which of the following statements about this reaction is correct? he reaction is only exergonic if enzyme is added b. The reaction is endergonic whether or not enzyme is added c. The reaction is exergonic whether or not enzyme is added d. The rate of oxygen production will be unaffected e. The reaction is only endergonic if enzyme is added
- Which of the following statements about a plot of V0 vs. [S] for an enzyme that follows Michaelis-Menten kinetics is false? a. As [S] increases, the initial velocity of reaction V0 also increases. b. At very high [S], the velocity curve becomes a horizontal line that intersects the y-axis at Km. c. Km is the [S] at which V0 = 1/2 Vmax. d. The shape of the curve is a hyperbola. e. The y-axis is a rate term with units of μm/min.The enzyme glutamine synthetase catalyzes the following reaction: glutamate + ATP + NH3 → glutamine + ADP + phosphate Which of the following statements about this reaction is correct? a. The reaction is endergonic whether or not enzyme is added b. The reaction is only endergonic if enzyme is added c. The reaction is only exergonic if enzyme is added d. The rate of oxygen production will be unaffected e. The reaction is exergonic whether or not enzyme is addedWhich of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply