Please correct answer and don't use hand raiting 1. Label I, II, III, IVIIEnergy levelIVIIIIProgress of reaction2. If A is original enzyme reaction state, and B and Cchemicals were added. What is the role of B and Cchemicals?PotentialEnergyAReaction Coordinate

Explanation for Question 1Labelling the Reaction Diagram:I (Reactants): This represents the starting…

Answered: 1. Label I, II, III, IV II Energy level…

Fundamentals Of Analytical Chemistry

9th Edition

ISBN:9781285640686

Author:Skoog

Publisher:Skoog

Chapter7: Statistical Data Treatment And Evaluation

Section: Chapter Questions

Problem 7.9QAP

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Calculate the specificity constant for an enzyme-catalyzed reaction if the total enzyme concentration is 15 nM, Vmax is 9 M/s, and Km is 150 M. A. Has the enzyme achieved catalytic perfection? (Y or N)
. Relation between Reaction Velocity and Substrate Concentration: MichaelisMenten Equation: At what substrate concentration would an enzyme with a kcat of 30.0s−1 and a Km of 0.0050 M operate at one-quarter of its maximum rate?
Please answer the calculation
Which of the following contributes most substantially to rate acceleration produced by an enzyme? O A. Ability to bind the substrate OB. Ability to bind the transition state O c. Ability to bind the product O D. All of the above contribute equally. 56
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?
Draw the mechanism
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
Please give handwritten answer of the both
Whethor or note the reaction will take place or not depends mainly on? 1. intricate structure of the enzyme. 2. equilibrium of a system. 3. presence of coenzyme. 4. amount of available substrate. 5. Gibbs free energy differences.
Q1: the following table gives the results of enzyme-catalyzed reaction. The enzyme concentration [E] = 0.00012 mmol/L Use the information of substrate concentration [S] and rate Vo for both experiments, with inhibitor and without inhibitor to answer the following questions (NOTE: [E] = 0.00012 mmol/L) [S], mmol/L 0.710 0.400 0.310 0.098 0.066 0.040 Experiment 11 without inhibitor VO, mmol/L-min 0.200 0.180 0.160 0.120 0.100 0.070 Experiment 2 with inhibitor [1] = 0.033 mmol/L VO, mmol/L-min 0.180 0.150 0.110 0.070 0.050 0.040 1- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs Vo 2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/vo 3- Calculate Kcat for the enzyme (without inhibition) 4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive)
Q1: the following table gives the results of enzyme-catalyzed reaction. The enzyme concentration [E] = 0.00012 mmol/L Use the information of substrate concentration [S] and rate Vo for both experiments, with inhibitor and without inhibitor to answer the following questions (NOTE: [E] = 0.00012 mmol/L) [S], mmol/L 0.710 0.400 0.310 0.098 0.066 0.040 Experiment 1 without inhibitor VO, mmol/L-min 0.200 0.180 0.160 0.120 0.100 0.070 Experiment 2 with inhibitor [1] = 0.033 mmol/L VO, mmol/L-min 0.180 0.150 0.110 0.070 0.050 0.040 1- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs Vo 2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/vo 3- Calculate Kcat for the enzyme (without inhibition) 4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive) Note:- show all your work to answer the above questions. Upload your answers…
Find [E] of total enzyme and change in concentration[E] with time of this reaction. E+S <-> (K1,K-1) ES <-> (K2, K-2)EP <-> E+P

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1. Label I, II, III, IV II Energy level IV I III Progress of reaction 2. If A is original enzyme reaction state, and B and C chemicals were added. What is the role of B and C chemicals? Potential Energy A Reaction Coordinate