Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Related questions
Question
Transcribed Image Text:### Understanding the Michaelis-Menten Plot
To improve comprehension of enzyme kinetics, refer to the Michaelis-Menten plot to answer the following question.
**Question:**
What is the estimated value of Vmax for the enzyme-catalyzed reaction (square data points)?
*(Choose the one best answer)*
- ○ 30 mM
- ○ 30 mM/sec
- ○ 60 mM/sec
- ○ 60 mM
Before answering, recall that Vmax is the maximum rate at which an enzyme can catalyze a reaction when fully saturated with substrate.
Refer to the accompanying Michaelis-Menten plot provided in your materials for detailed data points.
---
*Page Navigation:*
- Previous Page
- Next Page
*Page:* 20 of 36
Transcribed Image Text:### Michaelis-Menten Plot Analysis
#### Graph Description
The displayed graph is a Michaelis-Menten plot that depicts the relationship between substrate concentration and the initial velocity (Vo) of an enzyme-catalyzed reaction. The x-axis represents the substrate concentration in millimolar (mM), and the y-axis represents the initial velocity (Vo) in mM/sec.
- **X-axis (Substrate in mM)**: Begins at 0 and goes up to 300 mM.
- **Y-axis (Vo in mM/sec)**: Starts at 0 and progresses up to 60 mM/sec.
- **Data Points**: Square data points are plotted to show the relationship between the substrate concentration and the enzyme reaction velocity.
The graph shows a classic hyperbolic curve which is typical for Michaelis-Menten kinetics. As the substrate concentration increases, the reaction velocity rises rapidly at first and then approaches a maximum velocity (Vmax) asymptotically.
#### Educational Text
Use the Michaelis-Menten plot to answer this question: **What is the estimated value of Vmax of the enzyme-catalyzed reaction (square data points)?** (Choose the one best answer)
Based on the graph, it is observed that the reaction velocity (Vo) levels off as substrate concentration increases, approaching a maximum value. To estimate Vmax from the Michaelis-Menten plot, identify the asymptote (the horizontal line the curve approaches but never quite reaches) on the y-axis.
This graphical representation is crucial for understanding enzyme kinetics and determining vital parameters such as Vmax and Km (Michaelis constant), helping elucidate the catalytic efficiency and affinity of enzymes for their substrates.
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
Step by stepSolved in 2 steps
Knowledge Booster
Similar questions
- The following data were collected for an enzyme that can be described by Michaelis Menton kinetics. Use graphical analysis to determine the Km and Vmax for this exzyme / substrate combination. [S] mM Product formed (umol/min) 0.21 1.5 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45arrow_forwardThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…arrow_forwardFor some Enzyme, the Vmax is 18 micromols/min, Km is 400 microM. If the substrate concentration is 100 microM, what is the velocity of the reaction?arrow_forward
- Create a ONE page, formal summary, including APA Formatted in-text citations, of the enzyme amalyze and how it is used in the meat processing industry (Address all guiding questions below in your summary). Note, references can be the second page of the assignment. Include the questions in ur answer Which enzyme is used in the industry (if more than one enzyme is included, you can choose one of the enzymes) Describe the molecular structure of the enzyme (how many amino acids; discuss different levels of protein structure-secondary, tertiary, quaternary, key structural components/amino acids in active site) Describe how the enzyme works in the industry and why it is a key component for this industry. What specific reaction(s) are being catalyzed? What types of bonds are being broken?arrow_forwardCalculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme (lactase). (enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 per minute 0.25 per minute 0.50 per minute 1.25 per minute 5.0 per minutearrow_forwardIn mathematical terms, what characteristic of a graphed line is a measure of enzymereaction rate?arrow_forward
- Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.arrow_forwardFor an enzyme-catalyzed reaction, the velocity was determined at two different concentrations of the substrate. Estimate the value of Vmax. [S] (MM) 10 20 88 nmol/min 79 nmol/min 67 nmol/min V(nmol/min) 51 nmol/min 27 Not enough information is given to form a reasonable estimation. 48arrow_forwardPlease handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.arrow_forward
- Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.arrow_forwardFrom the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.arrow_forwardUsing the table below can you please help me answer the following. Based on your results, what can you conclude about the effect of enzyme concentration on reaction rate? Explainarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON