5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the ratesof reaction with glucopyranoside for various substrate concentrations was obtained. By constructing aLeaver-Burk plot, determine the value of the Michaelis constant.[S]/ (10-6 mol dm-3)v/ (10-3 mol dm-3 s-1)1.002.003.004.0016.733.341.149.8

Lineweaver-Burk Plot: This plot is also called as double reciprocal plot as equation for the plot is…

Answered: 5) In an experiment to investigate 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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The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change
The phosphoryl group transfer potentials for glucose-1-phosphate and glucose-6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? (b) If a mixture was prepared containing 1 m glucose-6-phosphate and 1 x 10-3 M glucose-1-phosphate, what would be the thermodynamically favored direction for the reaction?
1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
Determine the values of Km and Vmax for the decarboxylation of β-keto acid given the following data. Please show and label your plot. Show your calculations and box your final [S] in mol/l V in mM/ min 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256
Assume that the reaction Arabinose +Pi <> Arabinose-6-P has a delta G of +13.0 kJ/mol and the reaction XTP <> XDP + Pi has a delta G of -25.7 kJ/mol. Calculate the delta G for the combined reaction Arabinose + XTP <> Arabinose-6-P + ADP, in kJ/mol to four significant figures.
1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the inhibitor icreaces, what can be said about the mode of inhibition and why? 1.3) calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this? 1.4) discuss the mechanism of the bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues. make use of relavant graphs and diagrams to explain your answer.
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)
Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graph
Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?
Determine the values of KM and Vmax for the decarboxylation of a β-keto acid given the following data.

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