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

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

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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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 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
An enzyme has 10 times greater affinity for substrate "A" than for substrate "B". Which of the following is true? a.) KM of A is 10 times the KM of B b.) The concentration of B is 10 times that of A c.) Vmax of A is 1/10 the Vmax of B d.) KM of A is 1/10 the KM of B e.) Vmax of A is 10 times the Vmax of B
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
You are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?
A noncompetitive inhibitor (Circle one). a. Binds at the active site of the enzyme. b. Alters the three-dimensional structure of the enzyme. c. Increases the rate of the enzyme-catalyzed reaction. d. Has a structure similar to the substrate. e. Has its effect reversed by adding more substrate.
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 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
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.
Which of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.
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.
Which of the following statements about allosteric enzyme regulations are true. A. Allosteric regulations is always used to negatively regulate enzyme activity. B. Allosteric regulations are often end products of a biochemical pathway. C. Diffrent allosteric regulators turn enzyme activity on or off by binding the same site. D. Binding of allosteric regulators alters the conformation of an enzyme. B only B and C B and D D only A and D