A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below:[Substrate](MM)10305070▪ slope =▪ Vmax=▪ Km =Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor.▪y-int= [Select][Select]▪ Km =[Select][Select]Vo (mm/min)(without inhibitor)[Select]4.4310.2614.0716.73[Select]mM/minmMUsing linear regression analysis, determine the values of Vmax and Km of the enzyme in the presence of an inhibitor.▪ y-int= [Select]▪ slope = [Select]▪ Vmax=Vo (mm/min)(with inhibitor)✓mM/minmM2.606.068.239.73What is the type of inhibition involved? [Select]

Inhibitors inhibits the enzyme activity. There are three types of inhibitors-Competitive,…

Answered: A biochemist wants to determine the…

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

You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE, The kinetics data are shown below [Substrate, uM] Vo with DEDS M/min) Vo without DEDS (uM/min) M3.333 10.774, 11.196 14,000 0.877 1.316 5.000 1.012 #1.462 10.000 1.462 088'1 20.000 1.880 12198 Using linear regression analysis. deterane tievaluesof Vun K orthe ercymehine ABSENCE of inhibitoe Express your answer In 3 decimal places, do NOT include the units)
Consider the given data for an enzyme-catalyzed reaction. Determine the Vm, Km and the type of inhibition based on the given data below Substrate concentration, uM 30 50 100 300 900 slope y-intercept Complete the table below (include correct units). Experiment A Vm Km Experiment A (Initial velocity without inhibitor, uM-min) Type of Inhibition: 10.4 14.5 22.5 33.8 40.8 Experiment B (Initial velocity with inhibitor, uM-min) 5.1 7.3 13.3 25.7 37.2 Experiment B
You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE. The kinetics data are shown below: [Substrate, uM) Vo with DEDS (uM/min) Vo without DEDS (uM/min) 1.667 1.600 3.544 2.500 1.923 4.259 3.333 2.139 4.737 14.000 2.268 5.019 5.000 2.410 5.336 Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units) Vmax KM
The following data was obtained during kinetic analysis of an enzyme with and without an inhibitor. Substrate concentration (mM) Reaction rate without inhibitor (µM/s) Reaction rate with inhibitor (µM/s) 10 28 12 20 50 23 40 83 42 60 107 58 100 139 83 200 179 125 300 197 150 400 209 167 560 227 197 How do you calculate the KM for the enzyme in the absence of an inhibitor. And how do you calculate kcat with the given enzymatic concentration of 5 µM.
(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?
Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
Although graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction, sometimes these quantities can be quickly estimated by inspecting values of V0 at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained:
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?
The Lineweaver-Burke plot was originally developed in order to "linearize" the data obtained from enzyme kinetics experiments, in order to facilitate the determination of kinetic parameters. Why is it not considered to be an accurate method for this purpose? It is very difficult to draw a straight line on a computer. It is very difficult to calculate the variables required for the "x" and "y" axis. It is more accurate to use the standard "V versus [S]" plot to determine Vmax and KM- The plot weights the least accurate data points the most heavily. It is no longer considered to be acceptable to extrapolate from known data.
PA Enzyme (a) Earlier, the activity for this protein/enzyme was tested by monitoring the concentration of the product A' as a function of time. The results are shown in the table below. Copy these numbers into an excel spreadsheet and prepare an enzyme activity plot. Be sure to add all the necessary labels to your plot. (You don't need to copy the plot into this worksheet). Time (min) 0 1 2 3 4 567 A' 8 9 10 11 12 A' (μmol/mL) 0.0 11.0 22.1 33.1 44.1 55.1 66.2 77.2 88.2 92.4 94.5 96.6 96.6 (b) Which part of the data (in minutes) is suitable to use to calculate the activity of the Enzyme, and why? Write downs your answer in the space below.
Draw the isomers for each aldotetrose and ketopentose in the figure below and designate each isomer as a D or L sugar and designate also the R and S in every chiral centers. Label the enantiomers and diastereomers respectively. CH,OH C=0 Н-С—ОН Н-С—ОН Н-С —ОН Н-С—ОН ČH,OH ČH,OH

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