The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for anenzyme-catalyzed, single-substrate reaction E + S ES→ E + P. The model can be more readily understood whencomparing three conditions: [S] << Km, [S] = Km, and [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 enzymeconcentration and [Efree] refers to the concentration of free enzyme.[S] << Km[S] = Km[S] >> KmNot true for any of theseconditionsAlmost all active sites will[ES] is much lower than [Efree].be filled.The rate is directly proportional toIncreasing [Etotal] will increase[S].Km:Adding more S will not increase[Efree] is equal to [ES].the rate.

The Michaelis-Menten equation is represented as follows: V0 =VmaxSKm + S Initial velocity…

Answered: The Michaelis-Menten equation models…

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 Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for an enzyme-catalyzed, single-substrate reaction E + SES →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 V, where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Reaction rate is independent of [S]. Not true for any of these conditions The rate is half of the maximum rate.
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.
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V% 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 [ES] is much lower than [Efree]. Reaction rate is independent of Increasing [Etotal] will lower Almost all active sites will Km- be filled. [S). [Efree] is about equal to [Etotal]. Show All W- 5179933 (3).docx 5179933 (4).docx PCR-MINI RES....docx MacBook Pro
Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] [ES| k-1 + kz km Assume that k is negligible compared to the other rate constants. If the k is very small, it suggests that the enzyme has a Select an option affinity for its substrate, while if the if the km is very large, it suggests that the enzyme has a Select an option. affinity for its substrate. Select an option Submit You have used 0 of high Sav low moderate
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.
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.
The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
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.
The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/v) versus the reciprocal of the substrate concentration (1/[S]), is a graphical representation of enzyme kinetics. This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km. What term is represented by C? Linewegver-Burk Pt 1/Vmax O A. В. -1/Km Km/Vmax C.
Given the following reaction and equation for the initial velocity of the reaction: k₁ k3 E+S ES E + P V=Keat [ES] = k3 [ES] k₂ where keat is the rate constant for the reaction which forms the product from the ES complex. Explain in words why the velocity is directly proportional to theamount of enzyme added in the presence of saturating substrate levels.
In 1966, Ferdinand showed that a random-order ternary-complex mechanism for a two-substrate enzyme-catalysed reaction can lead to sigmoidal kinetics being observation in the absence of cooperative binding. Discuss this scenario so that it is clear why a plot of Vo versus [AXo] at constant [Bo] will be sigmoidal.
Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal for determining KM for an enzymecatalyzed reaction that follows Michaelis–Menten kinetics.

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