Q7: Answer Bank Suppose that you are working with an enzyme that has an ionizable active site residue with a pK₁ of around 6. The residue mustbe negatively charged for substrate binding and catalysis to occur. The reaction scheme is shown.SESE+ S+V+H*11EHWhich plot shows the expected pH dependency of the reaction velocity (Vo) when [S] = Km ? Drag and drop the correct plotinto the axes. Assume that the substrate is positively charged from pH 4 to pH 8 and that the Km was determined at pH 8.max4 5 6 7 8E +P+pHAnswer Bank

First let's name the curves as shown below, so that we can identify each of them using these…

Answered: Suppose that you are working with an…

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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An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
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
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.
An enzyme catalyzes a reaction at a velocity of 20 μmol/min when the concentration of substrate (S)is 0.01 M. The Km for this substrate is 1 × 10-5 M. Assuming that Michaelis-Menten kinetics arefollowed, what will the reaction velocity be when the concentration of S is 1 ×10-6 M?
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
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 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.
An enzyme catalyzes a reaction at a velocity of 20 micromole/min when the concentration of substrate (S) is 0.01 M. The Km for this 1 X 10^-5 M. Assuming that Michaelis-Menten Kinetics are followed, what will the reaction velocity be when the concentration of S is 1.0 X 10^-6 M?
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 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.
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.
Consider an enzyme that follows standard Michaelis-Menten kinetics and has the following kinetic constants: %3| k2 = 1.5 x 10? s1 Еo 3D 1 х 104 М = 1 x 104 M a. What is the value of the maximum rate VM? b. Prepare a hand-drawn quantitative plot on graph paper (not a simple sketch nor an EXCEL-generated graph) of the enzymatic reaction rate versus substrate concentration (like Fig 3-3) using the kinetic parameters given above. Be sure to label the axes and include numeric values on the axes. C. Based upon your hand drawn saturation plot, at what substrate concentration is the enzymatic reaction rate 75% of Vm?

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