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 briefly why. Km Km Substrate concentration [S] Do you observe a change in Vmax and Km in presence of competitive or noncompetitive inhibitor from the graph. Yes/No. Explain briefly why or why not с. Initial rate of reaction (v)

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 briefly why. Km Km Substrate concentration [S] Do you observe a change in Vmax and Km in presence of competitive or noncompetitive inhibitor from the graph. Yes/No. Explain briefly why or why not с. Initial rate of reaction (v)

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Please answer this question and the highlighted question is wrong please explain why and give me the correct answer
The effect of on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y) an allosteric effector a noncompetitive inhibitor a competitive inhibitor
Use graphs to illustrate enzyme activity as a function of the following: II. a. Substrate Concentration max velocity v max Rate Substrate Concentration b. Enzyme concentration Rate Enzyme Conc. с. рH Optimum Temperature Increasod temp. results in denaturation Rate Temperature d. Temperature Optimum pH Rate Increas ing pH
kcat is: a measure of the catalytic efficiency of the enzyme the rate constant for the reaction ES → E + P the rate constant for the reaction ES → E + S the [S] that half saturates the enzyme ½ Vmax
Don't give Handwritten answer
the Km of an enzyme for its substrate is 50mM. At what concentration of substrate would the enzymaticslly catalyzed reaction be at 60% maximum - 30 - 60 -75 - 50 -80
3
Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
Which class of enzymes have sigmoid or S-shaped plots of the rate of a reaction, v, versus the substrate concentration, [S], instead of the hyperbolic curves of the Michaelis-Menten equation? transferases holoenzymes O hydrolases O allosteric enzymes O ribozymes
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
When k2 >> k-1, KM approximates the affinity of the enzyme•substrate complex.The (circle one) higher / lower the KM, the more tightly the enzyme binds to its substrate
A competitive inhibitor interacts with the free enzyme to form an enzyme•inhibitor complex(E•I). This equilibrium reaction can be described as follows:E + I ⇌ EIModify the simplified kinetic scheme for the reaction E + S ⇌ E + P to include this equilibriumexpression