The steady-state kinetics of an enzyme are studied in the absenceand presence of an inhibitor (inhibitor A). The initial rate is given asa function of substrate concentration in the following table:v[(mmol/L)min-[S] (mmol/L)No inhibitorInhibitor A1.251.720.981.672.041.172.502.631.475.003.331.9610.004.172.38(a) What kind of inhibition (competitive, uncompetitive, or mixed)is involved?(b) Determine Vmax and Ky in the absence and presence of inhibitor.

Michaelis menten constant, Km is the substrate concentration required to produce half-maximum…

Answered: The steady-state kinetics of an enzyme…

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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The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Vo (micromol/min) Substrate added (mM) 200 1.0 400 2.0 800 4.0 1600 8.0 3200 16.0 The enzyme concentration used in all reactions is 106 M. Which of the following is true: O A) The Km for the reaction must be less than 1 mM ○ B) It is possible to determine Km for the reaction, but not Vmax or kcat OC) It is possible to determine only kcat, not Vmax or Km D) It is not possible to determine Vmax for the reaction OE) The ratio Vmax/Km for the reaction cannot be determined
In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM The inhibition occurred at 37.0°C. Assuming that the temperature increased to 37.5°C, what will happen to the Vmax and Km in the chemical system involving Inhibitor XYZ? Why do you say so? Provide illustrations using appropriate dimensions in the x and y axes. C.
In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM d. Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.
Use the Michaelis-Menten equation to complete the enzyme kinetic data set, whenKm is known to have a value of 1 mmol L−1 [S] (mmol L−1) Vo (μmol L−1 min−1) 0.5 50 1.0 2.0 3.0 10.0
Given the following equations of the line, a) determine the KM of the substrate that binds the strongest with the enzyme. b) determine which of the following substrates binds the least with the enzyme
Describe reaction between AP and PNPP and how is used to determine the kinetic parameters of AP. i. İndicate the value for the activity of AP(which is 3.08) What does it mean? Is your enzyme active or not? What does it say about the purity of your enzyme? ii. How the purification process affects the activity?
4.2
The 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?
Consider a general reaction enzyme A(aq) B(aq) The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C. Keg = What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is 0.50 M? 9:26 PM 35% 77°F 6/14/2021
Compound A is the substrate for two enzymes, El and E2, their reaction rates, r1 and r2,Determine the Km and rmax for both enzymes, with respect to the concentration of A. Which set of data is more likely to be for El and which for E2, and why? Concentration of 0.2 0.6 1.2 3 4 5 6 8 12 15 A (mM) Reaction rate (r.) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 Reaction rate (r,) (mmol/L*min) 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
The following data have been obtained for two different initial enzyme concentrations for an enzyme-catalyzed reaction. [E]=0.015 g/l) (g/l-min) [S] (g/l) v([E]=0.00875 g/l) (g/l-min) 1.14 20.0 0.67 0.87 10.0 0.51 0.70 6.7 0.41 0.59 5.0 0.34 0.50 4.0 0.29 0.44 3.3 0.39 2.9 0.35 2.5 a. Find K b. Find V for [E]=0.015 g/l. c. Find V for [E]=0.00875 g/l. d. Find k2. Use Eddie-Hostee plot to find your answer. Compare your result using Hanes- Wolf plot.
1) Is the ratio of the forward rate constant and reverse rate constant changed by the presence of an enzyme catalyst? 2) 4) What is the simplest mathematical relationship between substrate concentrations [S], initial velocity (Vo) of an enzyme catalyzed reaction, the maximal velocity of the reaction (Vmax), and the ½ maximal Vo (i.e. Km) ? (Hint: what is the Michaelis-Menten Equation? 3) Graphically illustrate the most useful derivation of the Michaelis-Menton equation (that darn linearized, double-reciprocal)

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