c) 1.0 1.2 Estimate Vmax and KM for all cases. What type inhibitor is [I]? Estimate K₁ and/or Kı' depending on the type inhibitor. Estimate K.cat. Estimate Kcat/KM.
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- 1). The initial velocity of an enzyme-catalyzed reaction has been determined at several substrate concentrations with and without an inhibitor I. The total enzyme concentration [E]ot present in each experiment is 1.20 x 10 M. [1] = 5.00 x10 M. (Note: v initial rate or velocity.) [S], M 1.25E-3 2.50E-3 5.00E-3 10.0E-3 v, M/min, no inhibitor 0.480E-3 0.660E-3 0.810E-3 0.920E-3 v, M/min, 5.00x10 M 9.43E-5 1.41E-4 1.70E-4 2.10E-4 b). What kind of inhibition occurred. c). Calculate the value of Ki = a). Use the Lineweaver-Burk plot to determine the values of Vmax and KM at [1] = 0.00 mM, and the values of Vmax and KM at 0.500 mM of I. it in 'How many molecules ofThe following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?The initial rates of an enzyme-catalyzed reaction have been determined for five different [S] (see table below). [S]o (mol.L-¹) 1.0 x 10 1.5 x 10-4 2.0 x 10-4 -4 5.0 x 10 7.5 x 10-4 -1 Vo (μmol.L-¹ min-¹) 28 35 42 63 75 1- Determine graphically the value of Km (first with the Michaelis-Menten representation and then with the Lineweaver-Burk representation, then compare by reporting on the Michaelis-Menten representation the values found by the Lineweaver-Burk representation) 2- Calculate the concentration of a competitive inhibitor 1, with a K₁ value of 2.4.104 M, whose action would quadruple the apparent value of Km.
- You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the Vmax to be 0.1 mol/sec and the Km to be 2.5 mM. What would the rate of the reaction be when the substrate concentration is 20 mM? 0.09 MS-1 O 0.133 Ms-1 O 0.18 Ms ¹ 9 Ms-1 O 0.018 Ms-1 0.2 MS-1You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseFrom the following data of an enzymatic reaction, determine the type of inhibition, the KM for the substrate and Ki for the enzyme-inhibitor complex. [S] mM 2.0 3.0 4.0 10.0 15.0 [P] mM/h (without inhibitor) 139 179 213 313 370 [P] mM/h ([I]=6mM) 88 121 149 257 313
- 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.Suppose that the data below are obtained for an enzyme catalyzed reaction in the presence and absence of inhibitor Y. [S] (mM) V (mmol/mL*min) Without Y With Y 0.2 5.0 2.0 0.4 7.5 3.0 1.8 10.0 4.0 1.0 10.7 4.3 2.0 12.5 5.0 4.0 13.6 5.5 a.) Determine the type of inhibition that has occurred b.) Does inhibitor Y combine with E, with ES or with both? Explain c.) Calculate the inhibitor constant, Ki, for substance Y, assuming that the final concentration of Y in the reaction mixture was 0.3mMGlucose can be isomerized to fructose to glucose isomerase. The enzyme kinetics of this enzyme was studied in the presence of an inhibitor X. Using the data provided, complete the table and determine what type of inhibitor is X. 1/ [S] , 1/M 1/V, w/o inhibitor Min/M 0.22 1/V, w/ inhibitor 0.33 0.27 0.2 0.16 0.20 0.14 0.13 0.16 0.11 0.11 0.14 0.09 0.11 0.13 Km/Vmax 1/Vmax Km Vmax
- Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.An inhibitor "I" is added to the enzymatic reaction at a concentration of 1.0 g/L. The data obtained are shown in the table below. No Inhibitor With Inhibitor [S](g/L) v ([E0] = 0,015 g/L) (g/L.min) v ([E0] = 0,015 g/L)(g/L.min) 40 2,28 1,818 20 1,74 1,316 13,4 1,4 0,986 10 1,18 0,76 8 1 0,62 (a)What kind of inhibition occurred?(b)Determine Ki (in g/L) for the inhibition of the previous exercise.