17.) In the left graph below, the dashed line (- - - -) represents what? В) Km A) Vmax C) equilibrium D) irreversible inhibition E) activation energy 18.) In the right graph below, the dashed line (- - - -) represents what? В) Кm A) Vmax C) equilibrium D) irreversible inhibition E) activation energy 19.) Based on the data table to the right, which of the substrates binds most tightly (highest affinity) to the enzyme? C) Nmemitip A) Masafime B) Vinasif D) Tanzora E) Kelplyn

17.) In the left graph below, the dashed line (- - - -) represents what? В) Km A) Vmax C) equilibrium D) irreversible inhibition E) activation energy 18.) In the right graph below, the dashed line (- - - -) represents what? В) Кm A) Vmax C) equilibrium D) irreversible inhibition E) activation energy 19.) Based on the data table to the right, which of the substrates binds most tightly (highest affinity) to the enzyme? C) Nmemitip A) Masafime B) Vinasif D) Tanzora E) Kelplyn

Introductory Chemistry: A Foundation

9th Edition

ISBN:9781337399425

Author:Steven S. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Donald J. DeCoste

Chapter21: Biochemistry

Section: Chapter Questions

Problem 28QAP: . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate...

See similar textbooks

Similar questions

. Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?
The conversion of CO(g) to CO₂(g) is sped up by introducing CO(g) to solid platinum. This makes platinum: A) A homogeneous inhibitor B) A heterogeneous inhibitor C) A homogeneous catalyst D) A heterogeneous catalyst E) None of the above
1. What is the role of initiator and inhibitor? 2. What are short stops?
Salicylate (aspirin) inhibits the catalytic action of glutamate dehydrogenase. You measure the activity of this enzyme in the absence and presence of the inhibitor. The data is presented in the table below. Substrate concentration (mM) Micrograms of product per minute, no inhibitor Micrograms of product per minute, 40 mM salicylate 0 0 0 0.5 0.11 0.04 1.5 0.23 0.09 2 0.27 0.1 3 0.32 0.12 4 0.36 0.13 8 0.45 0.16 16 0.5 0.18 In Microsoft Excel, generate the Michaelis-Menten graphs (i.e., the rate versus substrate concentration plots) for each of the inhibitor-free and the inhibitor-containing reactions. Without doing any calculation, and simply by visually observing the plots in Excel, estimate what the Vmax and the Km for this enzymatic reaction in the presence and the absence of the inhibitor. For Vmax, express your answer to one decimal place while using the appropriate rounding. For Km, express your answer to the nearest integer. Enter your answers in the table…
A4 Your enzyme is inhibited by one of the compounds depicted above. The inhibitor for your specific protein is indicated via the PDB protein code shown.On the basis of the enzyme’s structure, its substrate and mechanism of action, predict what type of enzyme inhibition ( i.e., competitive or non-competitive) may occur and justify why you think this is the case . (Up to 50 words) TYPE NOT WRITE.
We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor.I1,competitive inhibitor, I2,uncompetitive inhibitor, I3, non-competitive inhibitor.Assuming that Vmax = 80 mM s-1 , Km = 8 mM, and KI of all three inhibitors was 10 mM, which of the inhibitors was the most efficient on V0? Explain your answer
Enzyme X can act on either substrate A or B; the Km on A < Km on B. Vmax for A > Vmax on B.Sketch 1 plot for 1/v vs. 1/[S] plot for Enzyme X in the presence of A and in the presence of B.
Quesrion: Enzyme X exhibits maximum activity at pH = 10.5. X shows a fairly sharp decrease in its activity when the pH goes much lower than 9.5. One likely interpretation of this pH activity is that: a. A His residue on the enzyme is involved in the reaction b. a Glu residue on the enzyme is involved in the reaction c. a Tyr residue on the enzyme is involved in the reaction d. the enzyme uses NADH has a cofactor e. the enzyme uses coenzyme A has a cofactor Please explain why, thanks!
If we made a Lineweaver-Burk plot of an irreversible inhibitor, which type of reversible inhibition would it be most likely to resemble?
1. Solution Amount pH W 0.1 14 X 0.1 2.9 Y 0.01 2 Z 0.001 3 Which solution is prepared with weak acids.? 2. Why does changes in pH and temperature affect the efficiency of enzymes? A. Protein is altered. B. Changes in surfase are not recognizable. C. Activation energy is lowered. D. Enzymes work best in normal temperature and pH.
4-1Based on the experimental results shown in the table, Identify whether the inhibitor acting on this enzyme is acompetitive inhibitor or a non-competitive inhibitor, and Explain the reason logically. 4-2In 4-1, the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.
Two curves showing the rate versus substrate concentration are shown below for an enzymecatalyzed reaction. One curve is for the reaction in the presence of substance X. The other curve is for data in the absence of substance X. Examine the curves and tell which statement below is FALSE. A. X is an activator of the enzyme. B. The enzyme exhibits non-Michaelis-Menten kinetics. C. X is likely an allosteric effector. D. X is a competitive inhibitor