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…

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

What is the concentration of enzyme (in mM) needed to achieve a Vmax of 8.00 mM/s if the enzyme has a turnover number of 1.50s-1?
Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess uses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student searcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO hich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the neweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table Table 1. Enzyme Kinetic Data Velocity, mM/s Kmp 0.0351 [S], mM Cha Хan 0.492 0.0678 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Enzyme Kinetic Parameter: Parameters Vmax |Ku | Type of Inhibition Mode of Binding Xanthine Kaempferol Chlorogenic acid NA NA Line Weaver Burk Plot:
To purify a given enzyme from a crude extract that contains it, fractional precipitations, exchange chromatography are successively tested ionic and exclusion chromatography, with the results shown in the following table: Volume of dissolution Protein concentration Enzymatic activity (ml) (mg/ml) (U/ml) a) Calculate the percentage of recovery of the enzyme after each of the manipulations to which it has been subjected. b) Indicate if it is necessary to continue purifying the enzyme or if it is expected to have reached its electrophoretic homogeneity.
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
Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
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). 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.
Please explain each part thoroughly with explanations and answers given. This is Bipchemistry
8L.16.4
The rates at various substrate concentrations for an enzyme-catalysed reaction (b) are recorded as follows: 2.5 5.0 10.0 15.0 (S]/10 M 2.2 3.8 5.9 7.1 Vo/ M min Assuming the reaction obeys Michaelis-Menten kinetics, calculate the following values by using Lineweaver-Burk plot () maximum rate, Vmax- (i) Michaelis constant, Km- (ii) turnover number, kz.
With the help of the half reactions given in Table 1, formulate the redox equation for the oxidation of succinate and reduction of ubiquinone.
A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.
From a kinetics experiment, Kcat was determined to be 55sec^-1. For the kinetic assay, 0.05mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 30,000g/mole. Assume a reaction volume of 3mL. Calculate Vmax (um*min^-1) for the enzyme and catalytic efficiency (in M^-1sec^-1) for the enzyme. The Km for the enzyme was determined to be 8.3*10^-2M.

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