Please explain the formula (process) used to get the Red undelived numbers, Thanks!! example each Row, please. ISI 1/IS1
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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) 0.81. 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 28.25) 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
- The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function of substrate concentration in the following table: v[(mmol/L)min- [S] (mmol/L) No inhibitor Inhibitor A 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 (a) What kind of inhibition (competitive, uncompetitive, or mixed) is involved? (b) Determine Vmax and Ky in the absence and presence of inhibitor.1. Calculate the reaction Kcat for the Control in experiment (1). 2. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme.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?
- 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.Vmax [S] Vo = Km+ [S] Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km [S] Km 1 Vm Vm [S] The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For competitive inhibition The Michaelis-Menten equation becomes Vo=Vmax[S]/(aKm+[S]) Put the Michaelis-Menten equation for competitive inhibition in the Eadie-Hofstee format. The Y-intercept of this plot will be24. Researcher X did a series of experiments and determined the following about Enzyme A and its substrate (S). KM - 4 mM Vmax 100 mM/s axis. (. a) Draw the Michealis-Menton plot with all the above information shown. Be sure to label Vmax Rate of neation (mm) rate of react in mm. supstratiate concentration MM/S b) Convert the Michealis-Menton plot into a Lineweaver-Burk plot below, Label the axis. Vmax Rate of reaction (MM) 8 100 90 Go 100 80 - tmax 30 201 c) Using a dotted line, add in how á uncompetitive inhibitor how the rate would look with (S) (MM/S) x 1|S an uncompetitive inhibitor added. 100 KOMI Ke Vmax Vmar Sun competiti 6 • substante (MMIS)
- 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.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 be3. (a) The beakers below represent different conditions for measuring the initial velocity (vo) of an enzyme-catalyzed reaction under the steady-state approximation. The gray "donut-shaped" struc- tures represent the enzyme. The blue, filled circles represent free substrate molecules. The red cir- cles represent substrate molecules bound in the active site of the enzyme forming the Michaelis (ES) complex. Indicate in the diagram of the double reciprocal plot which kinetic parameters or variables each of the three "beaker conditions" represent either alone or in combination with another. A B 455 C V₁™¹ [So]-¹