enzyme e helps to catalyse the conversion of substrate s to product p which of the following parameters would change in response to increasing the concentration of E in this reaction - both the vmax and catalytic efficiency of enzyme e - the catalytic efficiency of enzyme e - both catalytic efficiency for E and affinity of enzyme e for substrate S - turnover number of enzymes - affinity of enzyme E for substrate S

enzyme e helps to catalyse the conversion of substrate s to product p which of the following parameters would change in response to increasing the concentration of E in this reaction - both the vmax and catalytic efficiency of enzyme e - the catalytic efficiency of enzyme e - both catalytic efficiency for E and affinity of enzyme e for substrate S - turnover number of enzymes - affinity of enzyme E for substrate S

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter7: Energy And Metabolism

Section: Chapter Questions

Problem 7TYU

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an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C
The Michaelis constant: depends on the concentration of the enzyme. displays the maximal rate of the reaction, when it is much less than the substrate concentration. displays the maximal rate of the reaction, when it is equal to the substrate concentration. displays zero-order kinetics, when the it is equal to the substrate concentration. describes the properties of the enzyme.
A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by: a) binding to a site other than the active site of the enzyme. b) binding to the active site of the enzyme, preventing substrate binding. c) decreasing kcat. d) Increasing KM.
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 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 state
Which 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 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.
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 correct
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... thx
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 false
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme?Select all that apply A.the active site of the enzyme must be rigid B.the active site of the enzyme must be flexible C.only one substrate could be converted to product by the enzyme D.the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures E.the entire enzyme must be rigid