Chemistry
10th Edition
ISBN: 9781305957404
Author: Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I
S] (uM) |
V (uM/min) |
|
|
without I |
with I |
3 |
10.4 |
4.1 |
5 |
14.5 |
6.4 |
10 |
22.5 |
11.3 |
30 |
33.8 |
22.6 |
90 |
40.5 |
33.8 |
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution
Trending nowThis is a popular solution!
Step by stepSolved in 4 steps with 5 images
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- 11. Applying the Michaelis-Menten Equation III Aresearch group discovers a new version of happyase, which they call hap- pyase*, that catalyzes the chemical reaction HAPPY = SAD. The researchers begin to characterize the enzyme. (a) In the first experiment, with [E] at 4 nM, they find that the Vnux is 1.6 M s, Based on this experiment, what is the kat for happyase*? (Include appropriate units.) (b) In another experiment, with [E] at 1 nM and [HAPPY] at 30 LM, the researchers find that V, = 300 IM s. What is the measured K of happyase* for its substrate HAPPY? (Include appropriate units.) (c) Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation and the two experiments repeated, the measured Vmax in (a) is in- creased to 4.8 uM S, pIM. For the inhibitor ANGER, calculate the values of a and o (d) Based on the information given…arrow_forwardUse the data below to determine the Michaelis-Menton constant [in mM] of a certain enzyme-catalyzed reaction. v = 0.152 mM/s at [S] = 0.334 mM v = 0.176 mM/s at [S] = 0.450 mMarrow_forwardquestion 19arrow_forward
- a. Using the graph paper below, to plot the enzyme velocity versus the substrate concentration in the absence of ibuprofen, estimate the Km and Vmax for this enzyme.arrow_forwardExhibit 8 for Question 30 Enzyme Enzyme Steady State Enzyme-Substrate Substrate Product Complex 30. The above diagram illustrates d. The relationship between the proteome and the metabolome The relationship between the concentration of enzymes and the rate of chemical reactions they е. catalyze f. a and barrow_forwardWhat parameters associated with enzyme activity are related to the Arrhenius equation? How can those parameters be plot to extract a relationship between them?arrow_forward
- Juan performed the same chemical reaction twice. His data from the first at- tempt is indicated by the red line. His data from the second attempt is indicated by the blue line. Energy During a Chemical Reaction Energy A B reactants e.g. C6H12O6 + O₂ C without enzyme Juan added pressure. with enzyme Reaction coordinate What change did Juan most likely make to his reaction the second time he per- formed it? activation energy with enzyme D Juan added a catalyst. Juan increased the surface area of the reactants. Juan cooled his reactants. activation energy without enzyme overall energy released during reaction products CO,+H,Oarrow_forwardConsider the following enzyme-catalyzed reaction: S - P Which of the following statements are correct: | When [S]>Km, the reaction rate will be determined primarily by the enzyme concentration and not the substrate concentration. | When [S]<arrow_forward8. Data on the speeds of a Michaelis-Menten enzyme reaction v (in micromolar/minute) as a function of the substrate concentration S (in micromolar) has been collected. Your goal is to find a model that fits this data. a) What type of transformation do you need to do for the data so that the transformed data looks like a linear function? b) Assume that the appropriate transformation on the data has been performed and that a linear regression line has been fitted to the transformed data and that its equation is given by Y = 0.501147.X +0.454986 Compute the parameters Vmax and KM and write the model. and KM = v(S) = micromolar minute c) What is the context domain of this function? d) Predict the speed of the reaction (in micromolar/minute) when the concentration is 12.45 micromolar. Round your answer to two decimal places. v(S) = micromolar minute e) What is the maximal speed of the reaction? micromolar minutearrow_forwardFor an enzyme that follows Michaelis-Menten kinetics, choose the best statement: O Vmax is completely independent of enzyme concentration. O Vmax can be attained as you add heat to the system. O Vmax can be approached but never truly attained. OVmax is attained at very high substrate concentrations.arrow_forwardWhich of the following is true for diffusion controlled reactions? a)The time required to break or form bonds is much more than the time required for the reactants to diffuse such that they are proximal to one another in the solution. b)The energy barrier associated with breaking or forming bonds is much higher than the barrier associated with the diffusion of the reactants to form the caged complex in the solution. c)Enzymes, at their initial stages of evolution toward a particular substrate, tend to operate at the diffusion limit. d)The rate of bond forming/breaking is much faster than rate required for a caged complex to separate.arrow_forwardKinetics questionarrow_forwardarrow_back_iosSEE MORE QUESTIONSarrow_forward_ios
Recommended textbooks for you
- ChemistryChemistryISBN:9781305957404Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCostePublisher:Cengage LearningChemistryChemistryISBN:9781259911156Author:Raymond Chang Dr., Jason Overby ProfessorPublisher:McGraw-Hill EducationPrinciples of Instrumental AnalysisChemistryISBN:9781305577213Author:Douglas A. Skoog, F. James Holler, Stanley R. CrouchPublisher:Cengage Learning
- Organic ChemistryChemistryISBN:9780078021558Author:Janice Gorzynski Smith Dr.Publisher:McGraw-Hill EducationChemistry: Principles and ReactionsChemistryISBN:9781305079373Author:William L. Masterton, Cecile N. HurleyPublisher:Cengage LearningElementary Principles of Chemical Processes, Bind...ChemistryISBN:9781118431221Author:Richard M. Felder, Ronald W. Rousseau, Lisa G. BullardPublisher:WILEY
Chemistry
Chemistry
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Cengage Learning
Chemistry
Chemistry
ISBN:9781259911156
Author:Raymond Chang Dr., Jason Overby Professor
Publisher:McGraw-Hill Education
Principles of Instrumental Analysis
Chemistry
ISBN:9781305577213
Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:Cengage Learning
Organic Chemistry
Chemistry
ISBN:9780078021558
Author:Janice Gorzynski Smith Dr.
Publisher:McGraw-Hill Education
Chemistry: Principles and Reactions
Chemistry
ISBN:9781305079373
Author:William L. Masterton, Cecile N. Hurley
Publisher:Cengage Learning
Elementary Principles of Chemical Processes, Bind...
Chemistry
ISBN:9781118431221
Author:Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:WILEY