To investigate the effects of a newly discovered inhibitor and enzymology list obtained the resultsshowed in the figure below.Which statement best describes the binding of its inhibitor on the enzyme?~y=0.768r+4.74253-0.568x+4657619....●xXThe inhibitor binds at the active site.The inhibitor binds away from the active site, but after substrate binding.The inhibitor binds away from the active site before or after substrate binding.The inhibitor binds close to the active site, but after substrate binding.The inhibitor binds close to the active site, but prior to substrate binding.red by a strain

Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Answered: ~0.766+ 47425 y-0.568x46576 . . . . . X…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.
the kinetics of an enzyme were analyzed in the absence of inhibitors, as well as in the presence of inhibitor A and inhibitor B. Using the given data below, construct or calculate the following (make sure the label graphs with appropriate axes and equations, and circle final answers) plot 1[S] as abscissa and 1/v as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots Calculate the; Km of enzyme in the reaction without inhibitor Km of the enzyme in the reaction with inhibitor (A dnB) Vmax of the uninhibited reaction Vmax of the inhibited reaction (A and B) What kind of inhibitor (A and B) was added to the enzyme-catalyzed reaction? Explain in terms of changes in Km and Vmax
Compare and contrast Bound Fraction equation in ligand binding and Michaelis-Menten equation in enzyme kinetics, including their double-reciprocal forms. Discuss what Km is important for and what Vmax (or kcat) is important for? Under what (substrate) conditions is Km more important than Vmax, and under what (substrate) conditions is Vmax more important than Km? Based on the discussions in question 2, explain what type of inhibitors works best under (a) high substrate concentration and (b) low substrate concentration.
Match the different names for inhibition mechanisms (1-5) with a description of their properties 7a-7d: 1. competitive inhibitor. 2. allosteric inhibitor also known as non-competitive inhibitor. 3. un-competitive inhibitor. 4. affinity label also known as active site directed covalent (irreversible) enzyme inhibitor. 5. Kcat inhibitor, also known as a mechanism-based covalent (irreversible) enzyme inhibitor. 4a. An enzyme inhibitor in which a substrate or competitive inhibitor is modified so that it contains a chemically reactive electrophile which can bind to and subsequently react with the enzyme active site: 4b. An enzyme inhibitor that contains latent reactive group that upon binding followed by catalytic turnover at the enzyme active site produces a reactive electrophile that reacts covalently with the enzyme: 4c. A reversible inhibitor that competes with the substrate for binding to the enzyme active site: 4d. A reversible inhibitor that can bind independently of substrate to its…
Glucose can be isomerized to fructose to glucose isomerase. The enzyme kinetics of this enzyme was studied in the presence of an inhibitor X. Using the data provided, complete the table and determine what type of inhibitor is X. 1/ [S] , 1/M 1/V, w/o inhibitor Min/M 0.22 1/V, w/ inhibitor 0.33 0.27 0.2 0.16 0.20 0.14 0.13 0.16 0.11 0.11 0.14 0.09 0.11 0.13 Km/Vmax 1/Vmax Km Vmax
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.
A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor C is: Uncompetitive TS‡ analog Mixed Inhibition Competitive Кмарр- Км 0 Non-competitive app - Vmax <0 <0 0 Vmax
Graph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information provided
1. Sulfanilamide, a sulfur drug, acts as an antibiotic. Explain its mechanism of action in the context of enzyme inhibition. 2. Methotrexate is used in cancer chemotherapy. Explain how this compound works by elaborating on the type of enzyme inhibition involved for its action. 3. For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. ( see attached picture ) 3a. how I and S bind to the E as shown by the Lineweaver Burk plot. 3b. the significance of the following obtained values for Km and Vmax. 3c. effect in slope and x-intercept
USSE EUSS reaction rate substrate concentration Blue line - Enzyme alone Red line - Enzyme + unknown compound The 4 graphs above represent the change in enzyme kinetics with the individual addition of different compounds that could be categorized as either: allosteric inhibitors, allosteric activators, competitive inhibitors, activators or non-competitive inhibitors. Review the graphs above. Each graph represents the activity of an enzyme and the enzyme + the addition of an unknown compound. By comparing the kinetics of the enzyme alone to the enzyme + unknown, determine what type of compound was added to each of the 4 different solutions to elicit the observed change.
Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o of 0.10 mM per minute when [S] = 0.125 mM, and a V o of 0.25 mM per minute when [S] = 0.50 mM)

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