36. On a lineweaver-Burk plot of kinetic data for an enzyme in the presence 1 x 10 M of a classic noncompetitive inhibitor, the y-intercept = 4 x 10M min and the x-intercept = -5 x 10' M'. What is the true Km of the enzyme? a. 2.0 x 10 M b. 2.5 x 10 M c. 1.2 x 10 M d. 0.8 x 10 M e. 1.2 x 107 M

36. On a lineweaver-Burk plot of kinetic data for an enzyme in the presence 1 x 10 M of a classic noncompetitive inhibitor, the y-intercept = 4 x 10M min and the x-intercept = -5 x 10' M'. What is the true Km of the enzyme? a. 2.0 x 10 M b. 2.5 x 10 M c. 1.2 x 10 M d. 0.8 x 10 M e. 1.2 x 107 M

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: Using the data provided use a Michaelis-Menten and Lineweaver-Burk plot to determine the K and Vmax…

A: The value of KM and Vmax for the given data is needed to be calculated using the Michaelis-Menten…

Q: . Derive an equation expressing v/Vmax \1-v/Vmax. as a function of log[S] for an enzyme that obeys…

A: An enzyme is a biocatalyst, which reduced the activation energy and increase velocity of a…

Q: Which of the following features in a Lineweaver-Burk plot is altered by a competitive inhibitor in…

A: The mechanism of an enzyme-catalyzed reaction was initially proposed by Michaelis and Menten and is…

Q: Label the diagram on the following slide: • 1. substrates • 2. products • 3. energy of activation…

A: In any reaction, reactant molecules need energy that is above their own energy amount in order to…

Q: Kinetic assays were performed to better understand the activity of the enzyme 245C in the absense…

A: The kinetic data is given for enzyme-substrate reaction in the absence and presence of a molecule B.

Q: 4. Derive a modified Michaelis-Menten equation for the following enzymatic reaction E+SES E+PEP…

A: The Michaelis–Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction.…

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: Michaelis-Menten analysis of enzyme kinetics has some limitations about the conditions under which…

A: The Michaelis-Menten equation is a mathematical model that describes the rate of enzymatic 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: QUESTION 13 Given the following data for an enzyme kinetics experiment. Determine the value of the…

A: 13.

Q: Bonus Question temperalures and the maximum reaction rate was determined from double reciprocal plot…

A: Some of the chemical reactions take place at a faster rate in the presence of a catalyst. In the…

Q: 0.04 0.07 0.0578 0.0867 0.1156 0.1445 0.10 0.12 0.1926 0.17 0.2407 0.22 0.2889 0.11

A: The surface area as, A=N' ×A1

Q: 0.0578 0.0867 0.1156 0.1445 0.1926 0.2407 02889

A: Freundlich isotherm equation as,

Q: What assumption does Michaelis-Menten kinetics use? a. The concentration of the substrate stays the…

A: The key premise is that the ES-complex concentration is stable. The velocity is also measured under…

Q: State

Q: Prograrr Potential Energy 100 150 200 250 300 350 400 450 500

A: Answer:- This question is answered by using the simple concept of calculation of energy using the…

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: PLEASE ANSWER THIS

A: From the given data, the values for 1/[S], 1/V without Inhibitor, and 1/V with inhibitor is…

Q: 6. The enzyme-catalysed conversion of a substrate at 25 °C has a Michaelis constant of 70 μmol dm3…

Q: N2 (g) + 3 H2 (g) 2 2 NH3 (g) + 100 KJ

A: Le Chatelier principal explained the effect of concentration, temperature and pressure on…

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: None

A: Step-1:To construct a Lineweaver-Burk plot and determine kcatk_{cat}kcat, follow these…

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: Cengage Learnin ✓ Cengage Learnin ✓ Cengage Learnin OWLv2 | Online ✓ b Cengage Learnin what are the…

A: The objective of the question is to calculate the activation energy (Ea) for the given reaction…

Q: In the cases where binding potency of the ligand A is determined in a functional assay in the…

A: The question is asking to define the relationship between EC50 for a ligand A and KD for a molecule…

Q: Reversible Enzyme Kinetics: Consider the following reversible reaction: k, k. E+S ES P+E k_1 Show…

Q: Jsing a fluorescent model substrate, you study the elow data. Write an equation describing reaction…

Q: After conducting an enzyme kinetics experiment, a student acquired the following linear equation…

A: Y=0.046x+0.72

Q: Identify the CORRECT statement regarding the chemisorption. A. Multilayer adsorption. B. Heat of…

Q: The following data were obtained for the adsorption of a certain material (ORA) on activated carbon…

Q: Ethyl lodide decomposes at high temperatures according to the reaction shown here: C2H5I(g) -…

Q: Chemistry The Km of an enzyme was increased from 75 μM to 150 µM in the presence of 0.5 µM…

A: Given Km(app) = 150 μM Km = 75 μM Inhibitor concentration, [I] = 0.5 μM Inhibitor constant, Kic =…

Q: Question 3 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is…

A: Note - Since you have asked multiple question, we will solve the first question for you. If youwant…

Q: The enzyme phosphomannomutase (PMM) binds to phosphate as part of its mechanism to phosphorylate…

A: Since you have asked multiple questions, we will solve the first question for you. If you want any…

Q: Identify the selected functional groups. Type the name of the functional groups In the boxes

Q: Examine the following image that provides a simple description of an enzyme-catalyzed reaction. E +…

A: Detailed explanation:Under saturating conditions, an enzyme-catalyzed reaction can reach a state…

Q: 8. Data on the speeds of a Michaelis-Menten enzyme reaction v (in micromolar/minute) as a function…

Q: 3. The kinetics of an enzyme with and without its inhibitor is shown in the plot below. 10 5 5 a.…

A: Kinetics of enzymes with and without inhibitors.

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: me Ksp equilibrium expression for lead(II) chloride is Pb₂Cl(s) 2Pb²+( 2Pb²+ (aq) + C¹-(aq). True…

A: Ksp equillibrium expression : It is the expression when a solid compound is written in equillibrium…

Q: 15.) On a Lineweaver-Burk plot, a changing y-intercept upon addition of increasing concentration of…

A: Enzymes are the specific catalyst that is used in biochemical reactions. The kinetics of enzymes is…

Question

e. urea
36. On a lineweaver-Burk plot of kinetic data for an enzyme in the presence 1 x 10 M of a classic
noncompetitive inhibitor, the y-intercept = 4 x 10M min and the x-intercept = -5 x 10' M'. What is
the true Km of the enzyme?
a. 2.0 x 10 M
M
b. 2.5 x 10
c. 1.2 x 10
M
d. 0.8 x 10
M.
e. 1.2 x 107 M

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

Construct a figure of Lineweaver-Burk plot. Determine the K, and Vmx of the enzyme- substrate complex from this figure. Please make sure that your figure has all the necessary components such as axis title, axis scale, axis unit etc. concentration (in mM) of substrate (NPP): 0.005mM 0.01mM 0.025mM 0.5mM 0.075mM 0.1mM 0.125mM p-nitrophenol (PNP): 0.00021mMmin-1 0.00023mMmin-1 0.00029mMmin-1 0.00043mMmin -1 0.00069mMmin-1 0.00028mMmin -1 0.00055mMmin -1
Below which is false about the Michaelis constant Km in Michaelis-Menten kinetics? k₂ k₁ E+SESE + P k₁ k₂ A higher K indicates a higher affinity between the substrate and the enzyme. Km is effectively equal to the Dissociation Constant (k_₁/k₁) for ES. When [Substrate] = Km, Vo = 1/2 V max When [Substrate] = Km [ES] = [Efree] = [Etotal]
4. Graphing the results from kinetics experiments with enzyme inhibitors The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [Er] is the same in each experiment. [S] (mM) 1 2 4 8 12 1 2 4 8 12 [S] (mm) a. Determine Vmax and Km for the enzyme. b. Determine the type of inhibition and the Kıfor each inhibitor. 1/[S] M-1 Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. and b. 1000 500 250 125 83.3 Answer: The data may be analyzed using double-reciprocal variables. For each [S] and corresponding u, we will calculate 1/[S] and 1/v. sed to get mo Helmien (1) v (μmol/mL sec 12 20 29 35 40 1/v (1) v (1) μmol/mL se mL-sec/umol C 12 20 29 35 40 Please explain how to get K 1/v 20 × 104 10 × 104 -400 8.33x104 5.00x104 3.45x104 2.86x104 2.50x104 Condition No inhibitor 0 5 mM inhibitor (2) 5 mM inhibitor (3) Plots of 1/v vs. 1/[S]…
The enzyme examase catalyses the following reaction, A - B where A is the reactant and B is the product A595 measurements were used to determine the catalytic activity of examase by measuring the rate at which B is produced. From this, the activity of the enzyme was determined to be 42 µmol/mL per minute. A standard albumin solution (concentration = 10 mg/mL) was used to prepare a standard curve of Abs595 vs amount of protein in mg. The protein assay was also performed using 100 uL of a 1 in 10 dilution of the original examase sample. For the absorbance measurements, it was determined that the sample used in the A595 measurement contains 1.2 mg of examase. Which of the following statements correctly gives the specific activity of examase? 1.0.35 U/mg O 2.0.035 U/mg 3. 5040 U/mg O 4.35 U/mg O 5.3.5 U/mg
Is the inhibitor competitive, uncompetitive or non competitive and why?
7
If 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, calculate the new Vmax. Calculate the new Km of the above lactase reaction, with inhibitor X. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. Inhibitor X exerts which of the following effects on the above enzyme (lactase)?
Ll.67.
Protein phosphatase 1 (PP1) helps regulate cell division and is a possible drug target to treat certain types of cancer. The enzyme catalyzes the hydrolysis of a phosphate group from myelin basic protein (MBP). The activity of PP1 was measured in the presence and absence of the inhibitor phosphatidic acid (PA). [MBP] (mg-mL-¹) 0.010 0.015 0.025 0.050 Vo without PA (nmol-mL-¹ min-¹) 0.0209 0.0355 0.0419 0.0838 Use the data in the table to construct a Lineweaver-Burk plot. What type of inhibitor is phosphatidic acid? Uncompetitive Noncompetitive Mixed inhibition Competitive Vo with PA (nmol-mL-¹ min-¹) 0.00381 0.00620 0.00931 0.01400
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
find the number of moles of acetic acid adsorbed per gram of C ?
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?