Enzyme X follows Michaelis-Menten kinetics. You add an inhibitor to your enzyme and you notice that theVmax has decreased while the Km for enzyme X has increased as a result of adding the inhibitor. What areyou able to conclude from this information?The inhibitor must be competitiveThe amount of total enzyme available to catalyze the reaction in the presence of the inhibitor has likely decreasedThe enzyme has a higher affinity for its substrate in the presence of the inhibitorThe substrate concentration required to reach 1/2 of the maximum velocity for this enzyme has increased as a resultof the inhibitorMore than one of the above are conclusions that can be drawn from this information

The Michaelis-Menten equation is used to describe the kinetics of enzyme catalyzed reactions. It…

Answered: Enzyme X follows Michaelis-Menten…

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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You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information provided
USSE EUSS reaction rate substrate concentration Blue line - Enzyme alone Red line - Enzyme + unknown compound The 4 graphs above represent the change in enzyme kinetics with the individual addition of different compounds that could be categorized as either: allosteric inhibitors, allosteric activators, competitive inhibitors, activators or non-competitive inhibitors. Review the graphs above. Each graph represents the activity of an enzyme and the enzyme + the addition of an unknown compound. By comparing the kinetics of the enzyme alone to the enzyme + unknown, determine what type of compound was added to each of the 4 different solutions to elicit the observed change.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo 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 Not true for any of these conditions Almost all active sites will [ES] is much lower than [Efree]. be filled. The rate is directly proportional to Increasing [Etotal] will increase [S]. Km: Adding more S will not increase [Efree] is equal to [ES]. the rate.
the kinetics of an enzyme were analyzed in the absence of inhibitors, as well as in the presence of inhibitor A and inhibitor B. Using the given data below, construct or calculate the following (make sure the label graphs with appropriate axes and equations, and circle final answers) plot 1[S] as abscissa and 1/v as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots Calculate the; Km of enzyme in the reaction without inhibitor Km of the enzyme in the reaction with inhibitor (A dnB) Vmax of the uninhibited reaction Vmax of the inhibited reaction (A and B) What kind of inhibitor (A and B) was added to the enzyme-catalyzed reaction? Explain in terms of changes in Km and Vmax
when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.
The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell?
Imagine a typical enzyme kinetic curve of [S] vs. V. The maximum [S] is about four times the Km. Lines are drawn at [S] = Km and V = Vmax. The asymptote is drawn at [S] = 0. 1. What effect does altering Km have on Vmax? Explain. 2. What effect does altering [E] have on Km? Vmax? Explain. 3. At what concentration of [S] is the initial velocity proportional to [E]? Explain.
What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
An uncompetitive inhibitor interacts with the enzyme•substrate complex to form a ternarycomplex (ES•I). This equilibrium reaction can be described as follows:ES + I ⇌ ESIModify the simplified kinetic scheme you drew for E + S ⇌ E + P to include this equilibriumexpression
How does the allosteric enzyme kinetics different from M-M kinetics? Draw a graph to show allosteric enzyme kinetics (initial rate vs [S]. Show how the graph change in the presence of + effector and negative effector.

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