An experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Resultsobtained are summarized in the table below.In all the experiments, the concentration of the enzyme is the same.Substrate ConcentrationVelocity(pmol/min)(pmol)1.50.2130.2840.320.3680.4150.45180.471. Plot or graph these results using the Lineweaver-Burk method.2. Determine the KM and Vmax values. Show all equations and calculations.

The enzymes are biomolecules that are vital for a biochemical to proceed at a faster rate. The…

Answered: An experiment on enzyme-catalyzed…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Given the following data in enzyme-catalyzed reaction, what is the Vm, Km and type of inhibition of Experiment A?
Can you please help me answer the following question in three paragraphs and in your own words. 1. How do you determine the effects of substrate concentration on enzyme activity? (Do not write a procedure just give as many details as possible. Please make sure this is at least in three paragraphs and in your own words).
Draw the Michaelis-Menten Plot and Lineweaver-Burke Plot of an enzyme in thefollowing situation. An enzyme, Enzyme A, has an optimal temperature at 34.5oC. The enzyme kinetic parameters were recorded to be Km = 15.0 μM, Vmax = 12.0 μM/s. The condition for an enzyme kinetic experiment has the temperature raised to 36.5oC. What will happen to the results? Provide at least five data sets prior to raising the temperature and after raising the temperature and plot the graphs as overlaying figures for comparison. Explain youranswer using a minimum of 200 words.
In an enzyme experiment, when the enzyme is added only to the substrate, the Vmax value is 0.828 and the Km value is 17.76. When the substrate and activator are added to this enzyme, the Vmax is 0.964 and the Km value is 10.6066. When substrate and inhibitor are added to the enzyme, the Vmax value is 0.550 and the Km value is 11.34. Estimate the effect of the substance added. Are these substances suitable activators/inhibitors for the laccase enzyme?
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.
The Km value of an enzyme-catalyzed reaction and its Vmax is 70 mmol/min. What is the rate of the reaction of the reaction when the substrate concentration is 7 × 10−2 mmol/min? a. 35 mmol/min b. 50 mmol/min c. 60 mmol/min d. 70 mmol/min
Given the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.
what is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.
The following were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Reaction Velocity (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 20 652 1000 The Km for this enzyme is approximately _____________. (Round to the nearest integer)
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions:(a). How do I determine the enzyme activity? Please give the unit. (b) How do I get the specific activity of this enzyme? Please give the unit.
The following questions deal with a fundamental understanding of enzyme catalysis.a. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of (ES) complex?b. What do you think is meant by saturation of the enzyme?c. What do you think is meant by the term “saturation kinetics”?d. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reachesa maximum value at high [S]?
Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?

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