9. For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in bothreactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitiveor uncompetitive.110-100-1/V a80-70-6030-40-3020-10-10. For your answer in #9, explain briefly:a. 1. how / and S bind to the E as shown by the Lineweaver Burk plot.b. the significance of the following obtained values for Km and Vmax.c effect in slope and x-interceptFoooF000

Enzymes are biocatalyst that increases the speed of reaction by lowering the activation energy. It…

9. 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. 110- 100- 90- 0- 70 60- 40- 20- 10- 10. For your answer in #9, explain briefly: a. 1. how / and S bind to the E as shown by the Lineweaver Burk plot. b. the significance of the following obtained values for Km and Vmax. c. ffect in slope and x-intercept Foo F0000 F0008 F0009 F000 Foo

9. 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. 110- 100- 90- 0- 70 60- 40- 20- 10- 10. For your answer in #9, explain briefly: a. 1. how / and S bind to the E as shown by the Lineweaver Burk plot. b. the significance of the following obtained values for Km and Vmax. c. ffect in slope and x-intercept Foo F0000 F0008 F0009 F000 Foo

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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2. The following mechanism has been proposed for superoxide dismutase. active site H*. H202 H20 (ii) H20 N-Zn H* O2 a. Explain each step in the catalytic cycle. b. What is the net reaction that occurs at this enzyme? c. Fe and Mn SOD’s exist in nature. What is the structure of each? How do their mechanisms differ from CuzZn2SOD?
5. An enzyme catalyzes the reaction M concentration of 1 nM, and the Vmax is 2 µM s-1. The Km for substrate M is 4 µM. N. The enzyme is present at a (a) Calculate kcat. (b) What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 2.0? Increased or decreased?
The time that is required for an enzyme to convert one substrate molecule into one product molecule is _________ A. Km. B. 1/kcat. C. 1/Km. D. kcat. Which of the following does not apply to the concerted model for subunit behavior: A. Each subunit can exist in a relaxed (R) and taut (T) conformation. B. All subunits will be in either the R or the T conformation at the same time. C. Some subunits can be in the R state while others are in the T state. D. The presence of inhibitors will lead to more of the enzyme being in the T form E. The presence of activators will lead to more of the enzyme being in the R form
Free Energy A+B a. Progress of the Reaction C. d. e. C+D A. Is the above reaction endergonic or exergonic? B. Which letter is AG of the reaction? C. Which letter is the activation energy of the enzyme catalyzed reaction? D. Which letter is the activation energy of the original reaction? E. If the above reaction has a AG of -3.6 kcal/mol could it be coupled to power kcal/mol?
answer from a to D a..Which of the enzyme has greater attraction for the subtrate b..Using the graph explain you enzyme in questionC..Which enzyme has greater maximum velocity (VMax）d .why doesnt the reaction rate continue to increase with subtrate concentration?
How can distance validate non-covalent interactions? Also, please explain if the distance between c-alpha of a particular residue in an enzyme and c-alpha of its ligand are 12.4 Å, 11.7 Å, 6.5 Å, 7.6 Å, and 7.7 Å, what does that mean? What is the meaningful distance, what is the legth of hydrophobic,hydrophilic, h-bond...?
PLEASE READ (CORRECTION): b.) Determine the type of inhibition imposed by inhibitor A and calculate Kic.) Determine the type of inhibition imposed by inhibitor B and calculate Ki
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.
Enzyme X has a Km for substrate A which is twice as large as its Km for substrate B. If the enzyme is added to a solution containing equal, but low concentrations of A and B and the Vmax for A and B are equal then: a. substrate A will be used exclusively. b. substrate A will be used at a rate greater than substrate B c. substrate B will be used exclusively. d. substrate A will be used at a rate equal to substrate B e. substrate B will be used at a rate greater than substrate A.
. H2 + CH2 = CH2 --> CH3CH3Which of the following could be a substrate for an enzyme that has an induced-fit active site and catalyzes the reaction above? a. CH3_OH b. CH2=CH_CH3 c. CH3_O_CH2CH3 d. none of the above
1. An enzyme-catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM s-1. What is the reaction velocity when the substrate concentration is 0.25 mM? 2. If an enzyme-catalyzed reaction has a velocity of 2 mm/min and a Vmax of 10 mm/min when the substrate concentration is 0.5 mM, what is the KM?
† 14.) A reversible inhibitor that is unable to bind to the ES complex A) always binds in the active site D) is always a noncompetitive inhibitor B) may be an uncompetitive inhibitor E) results in a decreased Kmapp C) results in an increased Vmax PP F) results in an unaltered Vmax pp † 15.) On a Lineweaver-Burk plot, a changing y-intercept upon addition of increasing concentration of inhibitor means C) the slope is increasing F) the Vmax PP is unchanged A) the inhibitor can bind to the free enzyme D) the inhibitor can bind to the ES complex B) the KmaPP is decreasing E) the Km PP is unchanged app 16.) Vn represents the rate of reaction for an enzyme-substrate pairing under what conditions? A) when [S] = ∞ E) for all [S]> Km max B) when [S] = Km F) for all [S] Km