Which of the following is incorrect? a. Without an enzyme, reaction rate can be increased by increasing the [reactants] Ob. Enzymes increase reaction rate by bringing the substrates to close proximity OC. A conformational change in an enzyme upon binding of a substrate is called "induced fit" Od. None; all the other choices are correct
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- Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called: Suicide substrates Transition-state analogs Both A and B Neither A nor Bwhich answer choice is correct im confused... thxWhich one of the following statements is true of enzyme catalysts? a. Their catalytic activity is independent of pH. b. They are generally equally active on D and L isomers of a given substrate. c. They can increase the equilibrium constant for a given reaction by a thousand fold or more. d. They can increase the reaction rate for a given reaction by a thousand fold or more. e. To be effective, they must be present at the same concentration as their substrate.Which statement is FALSE? a. For S P, a catalyst shifts the reaction equilibrium to the right. b. After a reaction, the enzyme involved becomes available to catalyze the reaction again. c. A reaction may not occur at a detectable rate even though it has a favorable equilibrium. d. Substrate binds to an enzyme's active site. e. Lowering the temperature of a reaction will lower the reaction rate.
- Which of the following is incorrect about enzyme cofactors? a. Some can be metal ions b. None; all the other choices are correct O c. The so-called co-substrates are needed in equal [substrates] and they are not recycled Od. Some are called coenzymes which are classified into co-substrates and prosthetic groups +The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.Which of the following statements is false? a. A reaction may not occur at a detectable rate even though it has a favorable equilibrium. b. After a reaction, the enzyme involved becomes available to catalyze the reaction again. c. For S → P, a catalyst shifts the reaction equilibrium to the right. d. Lowering the temperature of a reaction will lower the reaction rate. e. Substrate binds to an enzyme's active site.
- 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 stateA new drug has been discovered which inhibits the reaction catalyzed by enzyme A. The information on this drug is shown in the graph below. Based on this information, which one of the following is most correct about this drug? 1/No 2- inhibitor (0.1 uM] no inhibitor 11 1/[S), uM OA. competitive inhibitor binding to the substrate O B. competitive inhibitor binding to free enzyme A OC. uncompetitive inhibitor binding to [ES] O D. uncompetitive inhibitor binding to the Michaelis complex O E. allosteric enzymeWhich of the following statement/s is/are TRUE of enzymes? 1. They increase the rate of reaction by stabilizing the transition state. II. They raise activation energy to shift the equilibrium to favor the products. . They lower activation energy by altering the products of a reaction. O l and III O Il and III O III only o l only
- Which 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 applyI 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…A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme B