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)(pmol/min)1.50.210.2840.3260.360.4150.45180.471. Plot or graph these results using the Lineweaver-Burk method.2. Determine the Km and Vmax values. Show all equations and calculations.

One of the important models in enzyme kinetics to calculate the rate of enzymatic reaction is 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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Please 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.
Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
What is the initial velocity measurement for the hydrolysis of 50 μM amoxicillin by the enzyme?
The hydrolysis of a substrate, S, by an enzyme has been studied in the lab. The following initial rates, vo, were recorded at different concentrations. [S] (M) Vo (M/min) 2.10-10-4 1.20.10-6 4.20-10-4 3.10.10-6 9.30-10-4 6.30-10-6 1.42-10-3 9.10-10-6 A. Determine the rate constants for degradation of the substrate B. What is the rate of reaction at [S] = 1.1.104 M? C. Explain, why enzymes can make reactions go faster? Does enzymes also catalyse the reverse reaction from product to substrate?
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.
An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-
Concentrations in biochemical systems are often very dilute. Consequently, scientific notation and logarithms are often used to express concentrations. In scientific notation, numbers are expressed as coefficient x 10" To convert a number to scientific notation, proceed as follows: 1. Move the decimal place so that there is one digit in front of the decimal. 2. Account for the moved decimal in the value of x. If the decimal moved to the right, x is negative; if it moved to the left, x is positive. A logarithm is basically an exponent. Unless otherwise indicated, a logarithm is the a of 10". The numbers after the decimal point are significant; the number before the decimal just identify the location of the decimal point for the number. Notice that it is easy to estimate a logarithm from scientific notation; it's the exponent! Logarithms are commonly used to express the concentration of H. The pH is defined as pH= log (In), where the base number is 2.303. The same general rules as logs…
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
In a typical enzyme-catalyzed reaction, what are the relative concentrations of reactants and products as compared to the enzyme concentration?
For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?
The typical Michaelis-Menten equation mathematically describes the overall rate of the reaction as V (this is because biologists don't like math). What does V actually mean? (write the definition of V in differential equation form). V= d( )/dt Reaction rate Substrate concentration V max ·½V TURK
A continuous enzyme reactor consists of a stirred tank of volume 0.01 m3 through which liquid is pumped at 0.02 m3⁄h. The enzyme is immobilised onto non-porous, spherical support particles, and the contents are stirred well to ensure that the composition is uniform and that the particles remain in suspension. A plastic mesh has been placed in front of the exit pipe to prevent the particles from leaving the vessel. The reactor is used to carried out a 98% conversion of a substrate entering at 0.1 kmol m3 ⁄ . Michaelis-Menten kinetics apply, with the following enzyme characteristics: Turnover number = 1 × 10^3 s KM = 5 × 10−3 kmol m3 ⁄ Enzyme RMM = 65,000 (a) If the enzyme is stable, calculate the mass of enzyme that needs to be immobilised. (b) If the enzyme is not stable and experiences exponential denaturation with a half-life of 10 h at the reaction temperature, determine the denaturation constant. (c) How would you expect denaturation to affect the reactor performance?

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