Please provide the best possible work/ answers for the given problem. Attached is the starting bit of what the problem is referencing. This is Biochemistry. Thank you 4. Graphing the results from kinetics experiments with enzyme inhibitorsThe following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in thepresence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [ET] is the same ineach experiment.[S](mm)12(1)v (μmol/mL sec1220293540(2)v (μmol/mL sec4.38142126(3)v (μmol/mL sec5.594138161218Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. andb.a. Determine Vmax and Km for the enzyme.What type of inhibition does each inhibitor display? [S][S] mM124812no I#1umol/mL sec mM/min12202935404.38142126#25.591316181/[S]no I1/Vo#11/Vo#21/Vo

For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

4. Graphing the results from kinetics experiments with enzyme inhibitors The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [Er] is the same in each experiment. [S] (mm) 1 (1) v (umol/mL sec 12 20 29 35 40 2 4 8 (2) v (umol/mL sec (3) v (umol/mL sec 5.5 9 13 16 12 18 Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. and b. a. Determine Vmax and Km for the enzyme. What type of inhibition does each inhibitor display? 4.3 8 14 21 26

4. Graphing the results from kinetics experiments with enzyme inhibitors The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [Er] is the same in each experiment. [S] (mm) 1 (1) v (umol/mL sec 12 20 29 35 40 2 4 8 (2) v (umol/mL sec (3) v (umol/mL sec 5.5 9 13 16 12 18 Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. and b. a. Determine Vmax and Km for the enzyme. What type of inhibition does each inhibitor display? 4.3 8 14 21 26

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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8) plot of enzyme activity with and without an inhibitor present gave the following plot. What type of inhibitor is present? How does this inhibitor function? What changes are seen in Vmax and KM? Draw a line that approximates the result from addition of twice as much inhibitor to the reaction. 1/v (v in mM/min) 0.8 0.6 0.4 0.2 0 0.2 0.4 06 1/[s] ([S] in mM) 0.8
4. Graphing the results from kinetics experiments with enzyme inhibitors The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [ET] is the same in each experiment. [S] (mM) 1 2 4 8 12 1 2 4 8 12 [S] 1/[S] (mm) a. Determine Vmax and Km for the enzyme. b. Determine the type of inhibition and the Kifor each inhibitor. v (1) M-1 μmol/mL.se Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. and b. 1000 500 250 125 83.3 Answer: The data may be analyzed using double-reciprocal variables. For each [S] and corresponding v, we will calculate 1/[S] and 1/v. Please explain the formula (process) used to get the Red undelined numbers, example each Row, please. Thanks!! C 12 20 29 35 40 1/v (1) v (μmol/mL sec 12 20 29 35 40 -400 Condition No inhibitor → 20 x 104 1/v (1) mL sec/μmol 10 x 104 8.33x104 5.00x104 3.45x104 2.86x104 2.50x104 5…
The following kinetic data were obtained for an enzyme in the absence of an inhibitor (1) and in the presence of two different inhibitors (2) and (3) at 5mM concentration. [S], mM (mmol/mL/sec) (mmol/mL/sec) (mmol/mL/sec) (1) (2) (3) 1 12 4.3 5.5 2 20 8 9 3 29 14 13 8 35 21 16 12 40 26 18 Determine the Vmax and KM of the enzyme Determine the type of inhibition.
5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
1. A gluscose trasporter in teh liver cell binds with Km of 40mM. Calculate what fraction of vmax the Vo operating when blood glucose is 10mM 2. Draw a Michaelis-Menten kinetic curve and identify Vmax and Km. Indicate on the curve where the reaction is first order, where the reaction is zero order, where the reaction operates at half-saturation, and the range where most enzymes operate Be very clear about your labels.
1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 control) of enzyme inhibitor. Both inhibitors were added in each ИМ. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme. a. c. e. [S] (mM) (1) V. [(umol/(ml.s)] (2) V. [(umol/(ml.s)] (3) V. [(umol/(ml.s)] 7.6 4.4 6.6 4 14.6 8.6 11.4 26.6 16.4 17.8 16 45.8 29.8 24.6 24 60 40.8 28.2
KINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
12. Suppose an enzyme is known to obey Michaelis-Menten kinetics, but the parameters V and K are not known. Since two parameter values are missing, we might be able to find them by two independent measurements. So, suppose that two data points ( 51, Ri) (2 μΜ, 0.5 μΜ/s) and (82, R2) = (5 µM, 1 µM/s) are measured. By substituting the data points into the Michaelis-Menten law, find values of K and V that fit the data.
1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
Lineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km? Vmax = 5 umol min^-1, Km = 2.5 mM? Vmax = 5 mmol min^-1, Km = 25 M? Vmax = 5 umol min^-1, Km = 25 mM? Vmax = 5 mol min^-1, Km = 2.5 mM? Vmax = 5 mol min^-1, Km = 25 mM?
Vmax [S] Km + [S] Vo = Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km [S] Km 1 Vm Vm [S] 1 The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For uncompetitive inhibition The Michaelis-Menten equation becomes Vo-Vmax(S)/(Km+a'[S)) Put the Minchaelis-Menten equation for uncompetitive inhibition in the Lineweaver-Burk format. The slope of this plot will be