-0.04(1/v) (μM ¹s)0.080.01-0.010.060.040.020.04E + S3E + S₂E + S₁(1/[S]) (μM-1¹)Look at the graph above, comparing the data of three substrates binding to a single enzyme.What is the Michaelis constant (Km) of S1 binding to the enzyme?1/0.01-1/0.01 -0.04(swt) (A/I)0.080.06-0.0440.020.04E + S₁E+S₂E+S₁(1/[5]) (M¹)Michaelis-Menton data can be transformed into a double-reciprocal Lineweaver-Burk plot. The x-intercept on the Lineweaver-Burk plot corresponds to...+1/km-1/Km-1/Vmax+Kcat/Km

Answered: Image /qna-images/answer/5af53c34-5904-4e26-a70b-5c96c069179e.jpg

-0.04 (S_WH) (A/I) 0.08 0.01 -0.01 0.06 0.04 0.02 0.04 E + S3 E + S₂ E + S₁ (1/[S]) (μM-¹1) Look at the graph above, comparing the data of three substrates binding to a single enzyme. What is the Michaelis constant (Km) of S1 binding to the enzyme? 1/0.01 -1/0.01

-0.04 (S_WH) (A/I) 0.08 0.01 -0.01 0.06 0.04 0.02 0.04 E + S3 E + S₂ E + S₁ (1/[S]) (μM-¹1) Look at the graph above, comparing the data of three substrates binding to a single enzyme. What is the Michaelis constant (Km) of S1 binding to the enzyme? 1/0.01 -1/0.01

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...

See similar textbooks

Related questions

Q: 1. Reaction rate data of an enzyme, E, and a substrate, S, with increasing inhibitor concentrations…

A: Presented below is a comprehensive and step-by-step explanation, including with examples and…

Q: Reaction rate data of an enzyme, E, and a substrate, S, with increasing inhibitor concentrations are…

Q: None

A: Lineweaver-Burk Plot Basics:The Lineweaver-Burk plot is a graph that helps understand enzyme…

Q: 28. If an enzyme with a Vmax of 4.3 µmol.min', and a Km of 150 µM was investigated under pre-set…

A: The Michaelis- Menten equation helps in estimating the relation between the rate of the reaction and…

Q: Q18: 4. An in order of is used to elute proteins attached to a hydrophobic interaction…

A: •Given question is related to Hydrophobic interaction chromatography. •Hydrophobic interaction…

Q: Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee…

A: NOTE : FOR LINEWEAVER-BURK PLOT: THE SLOPE OF 1/V0 VS 1/[S] IS EQUAL TO FOR EADIE HOPSTEE PLOT:

Q: Consider the Michaelis-Menten equation and the definition of Km under steady state conditions. Under…

Q: 1. Determining Km and Vmax. You have recently discovered a new enzyme homeworkase which destroys…

A: The rate equation for Michaelis Menten equation is given as, R= K2SES +KM where,S = substrate…

Q: Which type of inhibitor is shown in the diagram? non-competitive inhibitor uncompetitive inhibitor…

A: Given options, Non-competitive inhibitor Uncompetitive inhibitor All…

Q: Based on the following plot, the KM for Enzyme A (shown in red) is type your answer... mM If this…

A: Enzymes are employed as catalysts during a chemical reaction to enhance the rate of the reaction.…

Q: What mutant of Dihydroorotase affected the most it's turnover rate? Estimate its impact on the…

A: The objective of this question is to show the mutants is one that has a significant effect on…

Q: 4. The following rate constants have been determined for a Michaelis –Menen enzyme: ki = 2.5 x 10$…

Q: None

A: EXPLANATION :Part 1 : Find expression of rate constant , rFirst of all in step one we have formed…

Q: Two students used the same enzyme and the same substrate to measure catalyzed reaction velocities…

A: “Since you have posted a question with multiple sub-parts, we will solve the first three subparts…

Q: The figure below shows the dependence of the enzyme's rate, v (in uM/min), as a function of…

A: Lineweaver–Burk plot gives the value of Vmax for the enzyme.

Q: 3. Use the equilibrium constants for reactions 1 and 2 to calculate Ke for reaction 3. (5 pts)…

Q: The equilibrium constant for the binding of a substrate to the active site of an enzyme was measured…

Q: Determine the kcat of the reaction given [E] = 2.5E-7 and the enzyme has a mass of kDa. (Km =…

A: The objective of the question is to determine the kcat of the reaction. kcat is the turnover number…

Q: 4. Suppose the data shown below are obtained for an enzyme catalyzed reaction. [S] (MM) v…

A: The equation is in the straight line, y=mx+b, form. So, we need to plot 1/V on y-axis and 1/[S] on…

Q: When studying the inhibition kinetics of a certain enzyme, the results have been obtained from the…

A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…

Q: The following results were obtained for an enzyme-catalyzed reaction Substrate concentration (mmol…

A: The objective of this question is to calculate the Michaelis-Menten constant (Km) and the maximum…

Q: If %T for sample A is 0.005%T and for sample B it is 25%T at 10 minutes after adding enzyme, which…

A: In the given question we have to choose the correct sample which shows the enzyme activity.…

Q: In a 250ul reaction containing 0.3 nmol of a Michaelis enzyme with Km = 4.4 x 10- M and saturating…

A: Given, Km=4.4×10-5M Initial velocity , Ve=6.3×10-3Mmin mol of Michaleis enzyme =0.3 nmol = 0.3×10-9…

Q: Complete the diagram of the mechanism of a general enzyme-catalyzed reaction. The abbreviations E,…

A: Detail description is given below

Q: Decompression sickness (also known as the bends) is a condition that affects divers and others…

A: Compounds containing covalent bonded atoms are known as covalent compounds. If the…

Q: Q14: What do X and Y axis represent? A) X axis is 1/[S] and Y axis is 1/[Vmax] B) X axis is 1/[Vmax]…

A: Graph which indicates the effect of competitive, uncompetitive, and noncompetitive inhibition of…

Q: If a substance is injected into the bloodstream, the percent of the maximum dosage that is present…

Q: answer from a to D a..Which of the enzyme has greater attraction for the subtrate b..Using the…

A: Enzymes : Enzymes are biocatalyst which increases the rate of biochemical reaction. Vmax : It is…

Q: In the Lineweaver-Burke plot below, which kinetic parameter(s) change upon addition of an…

A: The Lineweaver-Burk plot, also known as the double reciprocal plot, is a graphical method used to…

Q: 3. Calculate the pKb for thefollowing: a. Novocain, Kb = 7 x10-6 b. methyl red, Kb = 3 x 10-12

A: Here we have to calculate the pKb of the following given bases.

Q: a. Using the graph paper below, to plot the enzyme velocity versus the substrate concentration in…

A: Plotting the substrate concentration ([S]) on the x-axis and the enzyme velocity (V) on the y-axis…

Q: very strong back drugs on the tumor sizes of mice. The doctor is searching for the correct…

A: Rate of a chemical reaction is defined as the speed with which the reaction proceeds. It determines…

Q: Although there are accurate graphical methods available for determining Vmax and Km of an…

A: Approach to solving the question: Detailed explanation: Vmax and Km for the enzyme-catalyzed…

Q: Project 3 - kinetics The data below was collected with an enzyme, at a concentration of 10 nM, in…

A: Given data:

Q: Q7. Kinetics were analysed for an enzyme in the absence and presence of inhibitor. In the absence of…

A: A multiple choice question based on kinetics of reactions that is to be accomplished.

Q: Calculate the degree of ionization of paracetamol in the stomach (pH=1) and intestine (pH=5) Pka=…

Q: 1. Given the following data, determine the orders with respect to the concentrations of substances A…

A: The objective of the question is to determine the orders.

Q: In your kinetics assay, you combine 2.7 mL of 0.10 M NaCl and 0.2 mL of 30 µg/mL lysozyme dissolved…

A: In the kinetic assay method, the progress of the reaction is continuously measured as substrates are…

Q: If inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of…

A: Given: Reaction velocity (V0)1 = 0.10 mM/min [S]1 = 1.0 mM Reaction velocity (V0)2 = 0.133333 mM/min…

Q: In a certain culture where the rate of growth * of bacteria is proportional to the number present,…

A: We can calculate the initial bacteria number by using the formula b=bo e lambda ×t Where b = numbers…

Concept explainers

Applications of Molecular Spectroscopy

When light sources pass through the diffraction grating then light splits into different wavelengths. The light source produces two types of patterns that are shown as destructive and non-destructive. The light source is in the form of quanta that is quantitation.

Question

-0.04
(1/v) (μM ¹s)
0.08
0.01
-0.01
0.06
0.04
0.02
0.04
E + S3
E + S₂
E + S₁
(1/[S]) (μM-1¹)
Look at the graph above, comparing the data of three substrates binding to a single enzyme.
What is the Michaelis constant (Km) of S1 binding to the enzyme?
1/0.01
-1/0.01

-0.04
(swt) (A/I)
0.08
0.06
-0.04
40.02
0.04
E + S₁
E+S₂
E+S₁
(1/[5]) (M¹)
Michaelis-Menton data can be transformed into a double-reciprocal Lineweaver-Burk plot. The x-intercept on the Lineweaver-Burk plot corresponds to...
+1/km
-1/Km
-1/Vmax
+Kcat/Km

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Step by step

Solved in 2 steps with 2 images

SEE SOLUTION Check out a sample Q&A here

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

Hey what’s the answer to this
If the substrate concentration is twice the KM of an enzyme. The initial velocity (Va) is going to be of the maximum velocity (Vmax) according to Michaelis-Menten (MM) equation, Hint: Use the MM equation to arrive at the answer. O 1/2 O 1/4 O 1/3 O 2/3
A protein catalyzes the following reaction and had a Michaelis-Menten constant of Km=25 mM and a turnover number of 4.0 x 107 s-1. The total enzyme concentration is 0.012 µM and the initial substrate concentration is 4.76 µM. The enzyme has a single active site. Calculate the values of Vmax and V0 for this enzyme. 2H2O2 (aq) -----> 2H2O(l) + O2(g) Vmax= Vo=
Ll.67.
Consider the hypothetical enzyme-catalyzed reaction: A → B Given the kinetic data below, calculate the Vmax, in mM min-1, of the hypothetical enzyme for substrate A.
Hello, please answer the questions 1, 2, 3, and 4 clearly and directly.This is connected to Action of Catalase on Hydrogen PeroxideHello, please answer the questions clearly and directly.1. Using the equation E + S ⇆ ES → E + P, supply reaction involved in the experiment...2. How did you account for the physical observation of the action of catalase?3. Which of the enzyme specificity is represented by the experiment, conducted in the preliminary part? Why?4. State the optimum pH and temperature of catalase enzyme.
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute
how do we find reaction rate moles/sec using beers law? Determine the reaction rate in units of mol/sec using Beer's law. The extinction coefficient for pNP is: E = 1.8 x 10 Mcm Determine the reaction rates for the following enzyme concentration assays and enter them below. Rate for 1/2 Enzyme Concentration Rate for 2x Enzyme Concentration 2x Rare: 0.0039 Abs/see Assay 2x Rate; 0.0098 Abs/see Assy
How does Kcat influence the velocity of MM enzymes ? A. Linear relationship B. Inverse relationship C. No effect D. Only effects velocity if total enzyme concentration is low v = Vmax [S] KM + [S] Turnover rate kcat = Vmax [ET] Speed (substrates product/sec)
For an enzyme that follows Michaelis –Menten kinetics, k1=1X106 M-1 sec-1, k-1= 2x103 sec-1 and k2=2X 102 sec-1. a. What is the Km for the enzyme ? If the enzyme concentration is 10 nanomoles in 1 ml, what is Vmax for the enzyme ? What is the catalytic efficiency for this enzyme?
Match the units to each property for a biomolecular collision activation energy nm^2 collision frequency 1/s pre-exponential factor none kJ/mol reduced mass kg (or g/mol) collision cross-section 1/ (M s) steric factor >
What can contamination of reagents leads to? Unreliable results Reliable results Reproducible results Good results Catalase is the enzyme found in potatoes and It decomposes hydrogen peroxide (H202) to form water and oxygen gas. H202 + catalase - ----> H2O + 02 +E. The reaction is maintained at temperature 40 degree Celsius and there was a formation of bubbles. Based on the enzymatic reaction given, What do you think is the substance responsible for the formation of bubbles? Oxygen gas Hydrogen gas no reaction, because the enzyme catalase will be deactivated no reaction, because the enzyme catalase will be denatured Other: Based on the Fehling's test video, do you think the sugars ribose (in RNA) and the deoxyribose (in DNA) will both form a positive result (red precipitate) No Yes