Consider the following experimental data from another experiment:[S]1.52.002.505.0010.00V (No inhibitor)mmol ml¹ min¹0.1670.2040.2320.3130.385V (inhibitor)mmol ml¹¹ min¹¹0.1150.1430.1670.2500.333Calculate Km and V max and determine whether this inhibitor is competitive,non-competitive or uncompetitive.

Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…

Answered: Consider the following experimental…

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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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?
Suppose that the data shown in the margin are obtained for an enzyme -catalyzed reaction. [S] (mM) V (mmol/ml min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.00 1.0 8.33 2.0 9.09 a.) Determine the Km and Vmaxb.) Assuming htat the enzyme present in the system had a concentration of 10-6M, calculate the turn -over number
The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmol r'): 5.0 Initial velocity (umol l' min'): 6.67 10.0 20.0 40.0 147 182 233 323 400 Calculate Km and Vmax
Calculate, or make a best estimate of, the unknown factors in the situations listed in Table 1. Table 1. Data for problem 1. To find Data (i) Ek [K+]out = 4 mM; [K+]in = 130 mM (ii) [Cl-]in [Cl-]out = 570 mM; ECl = -65 mV (iii) ECl [Cl-]out = 150 mM; [Cl-]in = 8 mM; in a mammal (iv) [Na+]in Overshoot of action potential = +35 mV; saline [Na+] = 112 mM (v) [K+]in Blood [K+] = 3.2 mM; undershoot of action potential = -87 mV (vi) ECa [Ca2+]out = 5.6 mM; free [Ca2+]in = 0.8 mM (vii) [K+]out [K+]in = 350 mM; Ek = -82 mV
What is the change in concentration (umol/mL/min) for NADPH if the change in absolute absorbance per second from your DHFR functional assay analysis was 0.0035?
The concentration of hydrolyzed nitrocefin at each time point for an experiment is given below. Time (min) Concentration (μM) 0.5 6.01 1 11.78 1.5 17.6 2 23.51 2.5 29.58 3 35.31 3.5 39.73 4 44.5 4.5 48.18 5 50.05 5.5 52.72 6 54.01 6.5 55.06 7 55.65 7.5 56.39 8 56.74 8.5 57.49 9 58.03 9.5 58.61 10 58.69 Make a graph that plots the concentration of hydrolyzed nitrocefin (in μM) against time (in seconds) using Excel, R, SPSS or other computable software. Where appropriate, include a trendline that shows the linear range on your graph. Include the equations for the trendlines and the R2 value on the graph. Your graph should also include a title and appropriate titles for the x- and y-axes, with units included where appropriate. To determine the initial velocity of a possible insert in this experiment, you must determine what the linear range is in these data (see note below). Based on your graph, which time points represent a suitable linear…
Use the concept of Hess' Law to determine AH for the process V 2X +Z given the following numbered processes: V 2 W AH1 W X + Y AH2 Z- 2Y AH3 ΔΗ+ ΔH +ΔΗ3 ΟΔΗ+ 2ΔΗ-ΔΗ3 ΟΔΗ+ 2ΔΗ2+ ΔΗ3 ΔΗ + ΔH,-ΔΗ3
7.1 The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmolr'): Initial velocity (umol I' min"): 6.67 182 10.0 20.0 40.0 147 233 323 400 Calculate Km and Vmax
An enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
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
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

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