Which of the following statements is/are TRUE about the Lock and Key model of enzyme-substrate interaction? 1. The active site of the enzyme has flexible conformation. II. Only a certain number of substrates can fit on the enzyme's active site.
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- 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 correctWhich 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 onlyAn enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…
- Which of the following characteristics of the transition state is false? The number of noncovalent bonds increases between the enzyme and substrate at its transition state The transition state energy is part of the delta G ^0 for the reaction The energy required to reach the transition state is characterized by delta G (double arrow) The transition state is unstable due to the straining of the covalent bonds in the substrate Both answers B and C are falseMatch the definition to the term: v Choose... Temporary molecule that is formed when substrate attaches to the enzyme Substrate Product Compound that enters the reaction Substance that functions as a biological catalyst Enzyme Specific portion of the enzyme where the substrate attaches Result of enzyme reaction Active Site Enzyme-substrate complex Choose...Many pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false statement regarding enzyme inhibition. A- Enzyme can be inhibited by a ligand that binds to an active site B- Enzyme can be inhibited by a ligand that binds to a site other than that of substrate C- Enzyme can be inhibited by a ligand that forms a covalent bond with enzyme. D- It is true of all enzyme inhibitors, that the degree of inhibition is reduced when the concentration of inhibitor is lowered by metabolism or E- Enzyme may be inhibited by a ligand that does not bind in the substrate site
- 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…Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.Select all statements that are correct. Note there might be more than 1 correct statement. Competitive inhibitors bind to an allosteric side on the enzyme Uncompetitive inhibitors bind to the substrate binding site Competitive inhibitors bind to the substrate binding site Competitive inhibitors are usually of similar size and shape than the substrate of the enzyme Non-competitive inhibitors can bind to the free enzyme but not to the enzyme-substrate complex pe here to search C 6 D 88 20°C T ENG
- Select all the true statements about sequential versus concerted models of allostery. Group of answer choices A. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme B. No conformational changes occur in either model C. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding D. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formWhich of the following is incorrect? a. Without an enzyme, reaction rate can be increased by increasing the [reactants] b. Enzymes increase reaction rate by bringing the substrates to close proximity A conformational change in an enzyme upon binding of a substrate is called "induced fit" Od. None; all the other choices are correct OC.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.