Questions 2 through 4 refer to the figure below, which shows the reaction of an enzyme inthe absence and presence of various inhibitors.1/vB. BO C.CD. D1/[S]AWhich line best describes the activity of an enzyme in the absence of an inhibitor?O A.ABCD

The given graph has 1/v on y-axis and 1/[S] on x-axis. Therefore, it is a Lineweaver Burk Plot.The…

Questions 2 through 4 refer to the figure below, which shows the reaction of an enzyme in the absence and presence of various inhibitors. 1/v 1/[S] A Which line best describes the activity of an enzyme in the absence of an inhibitor? O A.A B. B OC.C D. D B C D

Questions 2 through 4 refer to the figure below, which shows the reaction of an enzyme in the absence and presence of various inhibitors. 1/v 1/[S] A Which line best describes the activity of an enzyme in the absence of an inhibitor? O A.A B. B OC.C D. D B C D

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Polymerization Kinetics

Polymerization is a chemical process in which one or more monomers combine to produce a very large chain-like molecule called a polymer. The functional groups present on the monomers and their steric effects are responsible for polymerization through a sequence of reactions that diverge in complexity. There exists a stable covalent chemical bond between monomers that sets apart polymerization from other processes. Polymerization is generally classified into step-growth and chain polymerization. Polymers are categorized into linear polymer and cross-linked polymers that are produced either by condensation or additional polymerization.

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Use the reaction energy diagram above to answer the following questions.
According to the following graph, the activity of the enzyme decreases more sharply at high temperature than at low temperature. What are the reasons for this observation? Enzyme activity Optimum temperature Temperature, °C I. As temperature is increased, the substrate binding slowly becomes poorer. II. As temperature is decreased, the enzyme moves more slowly and so reacts more slowly. III. At higher temperatures, the enzyme is denatured and stops working entirely. IV. Temperature has no effect on enzyme activity. ○ I only O IV only I and III O II and III
An enzyme has an optimal pH of 7.1 and an optimal temperature at 37° C. Which statement describes a reaction catalyzed by this particular enzyme at a constant temperature of 20° C? the reaction will slow down and then increase as the temperature increases O there is no effect O the reaction will be slower than if it ran at 37° C O the enzyme will provide an alternate active site so the reaction can proceed the enzyme will be denatured
What impact on k1 and k-1 would be when a mutation in the enzyme (E) makes the interaction between E and its substrate (S) stronger? a. k1 increase and k-1 decrease b. k1 decrease and k-1 decrease c. k1 decrease and k-1 increase d.
Why do most living organisms have an enzyme to decompose hydrogen peroxide? Ideal Gas and Decomposition of Hydrogen Peroxide Quiz Because hydrogen peroxide is present in many foods. Because hydrogen peroxide is toxic and needs to be destroyed. Because hydrogen peroxide does not dissolve in water. Because hydrogen peroxide is produced in the liver.
The following graph represents the results of an experiment onta metabolic enzyme. What is the optimum pH of this enzyme? click here if need to download image 3 456789 10 pH O 5.5 O 9.5 O 3.0 O 6.5 rate
Question #44
The peak on the blue line marked by the #2 represents which of the following? Free energy, G Transition state (‡) S 2 3 ES EP 4 AG* P uncat Reaction coordinate JAG cat The energy required for the enzymatic conversion of substrate to product. The binding energy (AGB) of the substrate binding the enzyme. Desolvation of the substrate and the active site of the enzyme.. Solvation of the product and the active site of the enzyme..
Allosteric regulators alter the equilibrium between the: A. ES state B. R and T forms of an enzyme. C. forward and reverse reaction rate. D. formation of the product and its reverse reaction. E. concentration thresholds.