What does the Michalis-Menten equation tell you?A. The velocity of an enzyme under physiological conditionsB. The variation of enzyme activity as a function of [substrate]C. The quantity of reactant that disappears per unit timeD. A and BE. B and CVo=Vmax [S]KM + [S]Vo=Vmax®[S]KM + [S]

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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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Which of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to work
During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded: a. Determine the Michaelis-Menten constant for the reaction with no inhibitor present at 30 °C and at 49.6 °C. b. Determine the maximum velocity of the uninhibited reaction at 30 °C and an enzyme concentration of 1.6 g/L. c. Determine the Ki for the inhibitor at 30 °C and decide what type of inhibitor is being used.
The following reaction sequence consists of two different substrates catalyzed by an enzyme:let's assume he described his reactions.;E + S1: ES1ES1 + S2: ES1S2ES1S2 → P + Ea.Derive the reaction velocity equation with Michaelis-Menten acceptance.b. Derives the rapid equality of S1 substrate concentration, rather than S2 substrate concentrationsimplify for reaction cards where it is higher.
a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your work
Shown below is Lineweaver-Burk plot for an enzymatic reaction at different substrate concentrations in the presence and absence of an inhibitor. The enzyme concentration is identical in both reactions: 1/v (sec/mM) 4.5 4 3.5 3 2.5 2 1.5 1 0.5 0 0 0.2 0.4 y = 0.997 +3.01x (+1) 0.6 1/[S] (mM-¹) y = 0.09999 + 3.01x 0.8 (-1) 1 (c) What is the type of inhibition mechanism? A. competitive inhibition B. uncompetitive inhibition (substrate-dependent) C. mixed inhibition (a) Does this enzyme obey Michaelis-Menten kinetics? (yes or no) Explain: D. noncompetitive inhibition (substrate-independent) E. allosteric inhibition 1.2 (b) What are the apparent values of Vmax and KM for each experiment (with and without inhibitor)? d) If the concentration of the inhibitor is 0.1 mM, what is the value of KI and/or K'I (whichever is relevant)?
The Lineweaver - Burk plot (Figure 1) shows an enzyme-catalyzed reaction in the absence and presence of 0.1µM inhibitor (ketoconazole). O Estimate Vmax and Km in the absence and presence of the inhibito.. (ii) Determine the type of inhibition shown by the inhibitor. Explain. 0.1- 0.08 0.06 - With inhibitor 0.04 0.02 Without inhibitor 0.4 -0.2 -0.02 0.2 0.4 0.6 0.8 1.0 1/{S\(&M-1) 1/vo (pmol-11 min)
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V₁ for an enzyme-catalyzed, single-substrate reaction E + S ⇒ ES →→ E + P. The model can be more readily understood when comparing three conditions: [S] > Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Almost all active sites will be filled. Adding more S will not increase the rate. Answer Bank Not true for any of these conditions Increasing [Etotal] will lower Km.
a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.
(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90
a. 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). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme. c. (1) V. [(umol/(ml.s)] 7.6 (2) V- Τ (μmol/ (ml.s)] [S] (mM) (3) V. [(umol/(ml.s)] 6.6 2 4 14.6 26.6 45.8 4.4 8.6 16.4 29.8 11.4 17.8 24.6 28.2 16 24 60 40.8
L(24 points) Explain How is the Michaelis constant defined. and what does a low or high value for Km tell you? What is the difference between the velocity and initial velocity of an enzyme reaction? What determines the efficiency of an enzyme reaction, and what terms are used to describe it? 2. (50 points) About how to obtain kinetic data experimentally Lisa decides to obtain values for the Km and Vmax of an enzyme she has just isolated from liver cells (it is now pure), using a Michaelis Menten plot. Describe in detail what kinds of measurements she would have to make, and what she would need to plot on graphs in order to estimnte the values for Km and Vmax. (Show the kinds of graphs she would have to plot, and how these will allow her to estimate Km and Vmax.) Describe how she would be able to obtain Vmax experimentally and from the Michaelis Menten plot - what conditions are needed and what would be measured). Also, describe what she would have to do to obtain the turnover number of…
By using Excel or GoogleSheets, graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and V values for the inhibited and uninhibited reactions? Is the inhibitor competitive or max noncompetitive? [S] (mM) V, No Inhibitor (mmol min-') V, Inhibitor Present (mmol min-') 1× 10-4 5 × 10-4 1.5 × 10-3 2.5 × 10-3 5 × 10-3 0.026 0.092 0.136 0.150 0.010 0.040 0.086 0.120 0.165 0.142 Activate

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