b. Evaluate the kinetic parameters (maximum velocity (Vm), Michaelis-Menten constant (Km),and turnover number (Kcat)) and justify the selection of temperatures based on the kineticparameters calculated. Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillusniger at different temperatures in the production of glucose from maltodextrin. The rates ofreaction measured are using an enzymes concentration of 0.003 μmolml-¹.Table 1: Glucoamylase Activity at different temperaturesMaltodextrin Concentration(μmol/L)0.511.52.25.511Initial Reaction Velocity(μmol/L.s)T = 40°C2.13.54.95.65898.39.3T = 60°C5.29.713162331

Enzymes catalyse the biochemical reactions by decreasing the activation energy. Enzyme kinetics are…

Answered: Table 1 shows the kinetic data that…

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter6: Basic Clinical Chemistry

Section6.5: Blood Glucose And Hemoglobin A1c

Problem 8RQ

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Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-1. Outline and describe the reaction scheme of the production of glucose from maltodextrin by using glucoamylase.
Calculate the mass of invertase (in mg) and concentration of invertase (in mM) contained in a 25.0mL sample of yeast extract that has 3,000 total units of activity, assuming that pure invertase has a specific activity of 1,000 units/mg with a mass of 270kD.
For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142
Conversion of F1,6BP to GA3P and DHAP by aldolase is striking in that it is strongly unfavorable when all species are at 1 M (∆G°’ = +22.8 kJ/mol) but favorable when the species are at their physiological conditions (∆G = -5.9 kJ/mol). Based on ∆G°’ and ∆G of aldolase and TIM, and using a reasonable physiological value of 15 mM for the concentration of F1,6BP, calculate the concentrations of GA3P and DHAP under physiological conditions (use T = 37°C). Why is the reaction so much more favorable under these conditions than when all species are at 1 M?
The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?
The KM for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8 × 10−2 M, and the KM for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6 × 10−4 M. (a) Which substrate has the higher apparent affi nity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax?
Calculate the standard free-energy change of the reaction catalyzed by theenzyme phosphoglucomutase, given that, starting with 20 mM glucose 1-phosphate and no glucose 6- phosphate, the final equilibrium mixture at 25 °C and pH 7.0 contains 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. Does the reaction in the direction of glucose 6-phosphate formation proceed with a loss or a gain of free energy?
The following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0
The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). [S], M V w/o inhibitor, M/s V w/ inhibitor, M/s 1x10-4 0.0259 0.0098 5x10-4 0.0917 0.040 1.5x10-3 0.136 0.086 2.5x10-3 0.150 0.120 5x10-3 0.165 0.142 In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.
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 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"

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