B 2B 1/A O Single Substrate Reaction O Random Single-Displacement Reaction Ordered Single-Displacement Reaction O Ping-Pong Reaction A/I
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- PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4Match the following terms with the best definition. Enzyme Product Substrate Active Site A. A macromolecule serving as a catalyst. B. A material resulting from a chemical reaction. C. The reactant on which an enzyme works. D. Location on an enzyme where the reaction is catalyzed.Define the following terms: a. velocity b. kinetics c. half-life d. first-order reactions e. pseudo-first-order reaction
- Identify the conditions that may affect enzyme activity in a reaction. SELECT ALL THAT APPLY A. Increasing Temperature B. Decreasing Substrate C. Lack of coenzyme D. Decreasing pHWhich of the following statements is FALSE regarding all reactions of the type A <=> B at equilibrium? a) net velocity (V) = 0 b) V of forward reaction = V of reverse reaction c) kf = kr d) ∆Gactual = 0Which statements concerning free energy change are true?a. Free energy change is a measure of the rate of a reaction.b. Free energy change is a measure of the maximum amountof work available from a reaction.c. Free energy change is a constant for a reaction under anyconditions.d. Free energy change is related to the equilibrium constantfor a specific reaction.e. Free energy change is equal to zero at equilibrium.
- Use the following graph to diagram the energetics of a chemicalreaction, with and without an enzyme. Be sure to position reactantsand products at appropriate points and to indicate the stages in thereaction and the energy levels.Sketch on one reaction rate vs. substrate concentration graph & sketch on one Lineweaver-Burk type plot the following:a) A Michaelis-Menten enzyme with a Vmax = 60 1/s and a KM = 125 M.b) An uncompetitive inhibitor of the enzyme described in a).c) An allosteric enzyme with the same Vmax as the enzyme described in a) and follows the sequential modelWhich of the following statements helps best explain the reaction specificity of an enzyme? a) The shape and charge of the substrates are compatible with the active site of the enzyme. b) The free energy of the reactants is greater than the free energy of the products. c) The equilibrium constant of the reaction is much greater than 1. d) The concentration of the enzyme inside living cells is greater than the concentration of substrate.
- 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 6Which of the following steps should be followed when performing kinetics experiments? the michaelis constant must be known the enzyme and substrate should not be mixed until just before the absorbance readings are taken reaction rates must be taken until reaction completion enzyme concentration must remain constantMatch each reaction description to the type of enzyme that catalyzes the reaction. 1. Oxidation and reduction of compounds 2. Transfers a functional group from one compound to another compound 3. Utilizes water to break bonds within a compound 4. Addition/removal of a group of atoms and bonds within a compound 5. Forms a bond between two compounds A. Ligase B. Transferase C. Hydrolase D. Oxidoreductase E. Isomerase F. Lyase