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    M4 Assignment

    Uploaded by

    James Bui
    Vmax = 1428.57 m/min Km = 79.316 μM

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd

    M4 Assignment

    Uploaded by

    James Bui
    421 views4 pages
    Vmax = 1428.57 m/min Km = 79.316 μM

    Original Description:

    UC Berkeley Module 4 assignment

    Original Title

    M4assignment

    Copyright

    © © All Rights Reserved

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    PDF, TXT or read online from Scribd

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    Vmax = 1428.57 m/min Km = 79.316 μM

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    421 views4 pages

    M4 Assignment

    Uploaded by

    James Bui
    Vmax = 1428.57 m/min Km = 79.316 μM

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    You are on page 1of 4

    Question 1: The reaction for the cleavage of fructose 1,6-bisphosphate to dihydroxyacetone

    phosphate and glyceraldehyde 3-phosphate is catalyzed by the enzyme fructose 1,6-bisphosphate


    aldolase and has a standard free energy change of ΔG°′ = +23.8 kJ/mol.

    A. What is the Keq of the reaction at 37 oC? (R = 8.314 J/°mol)?

    1.

    2.

    3.

    4.

    5.

    6.

    7.

    8.

    9.

    10.
    B. If the intracellular concentration of fructose 1,6-bisphosphate at equilibrium (ΔG = 0) was 10
    mM, what would be the predicted concentration of the products?
    [ ]
    1. [ ]

    [ ]
    2. [ ]
    – multiply both sides by 10

    3. [ ]

    C. In cells, the reaction catalyzed by fructose 1,6-bisphosphate aldolase readily occurs to


    produce dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Why do you think
    this is the case especially since the aldolase reaction has a large positive ΔG°′ = 23.8
    kJ/mol?

    1. Although the ΔG°′ is positive this does not represent physiological conditions. Under
    standard physiological conditions, the concentration of fructose 1,6-bisphosphate
    aldolase is much higher than the products dihydroxyacetone phosphate and
    glyceraldehyde 3-phosphate. This results in a ΔG that is close or below zero, which
    allows the reaction to proceed.
    Question 2: You have just discovered a new enzyme that catalyzes the degradation of cellulose to
    glucose. You hope to commercialize this enzyme ultimately to invent a process for biofuel
    manufacture. In order to determine how efficient the enzyme is and how fast the enzyme catalyzes
    the reaction, you have to perform some basic enzyme kinetics. Plot the following enzyme data for
    the enzyme catalyzed reaction and determine the Km and Vmax. (4 points)

    Enzyme Data for the Enzyme Catalyzed Reaction

    Substrate (cellulose)
    Rate of conversion from cellulose to
    Concentration (µ molar 1/S 1/V
    glucose (m/min)
    concentration)

    0 0

    6 98 0.1667 0.0102

    15 230 0.0667 0.0043

    24 390 0.0417 0.0026

    50 600 0.0200 0.0017

    95 680 0.0105 0.0015

    180 700 0.0056 0.0014

    Enzyme Data for the Enzyme Catalyzed Reaction


    800
    Rate of conversion from cellulose to glucose (

    700

    600

    500
    um/min)

    400

    300

    200

    100

    0
    0 20 40 60 80 100 120 140 160 180 200
    Substrate (cellulose) Concentration ( umolar concentration)
    Lineweaver-Burk plot of Enzyme Data for the
    Catalyzed Reaction
    0.0120
    y = 0.0561x + 0.0007
    0.0100

    0.0080
    1/V

    0.0060

    0.0040

    0.0020

    0.0000
    0.0000 0.0200 0.0400 0.0600 0.0800 0.1000 0.1200 0.1400 0.1600 0.1800
    1/S

    Determination of Vmax

    1. Y-Intercept = 1/Vmax
    2. 0.0007 = 1/Vmax
    3. Vmax = 1428.57

    Determination of Km

    1. Slope = Km/Vmax
    2. 0.0561 = Km/1428.57
    3. Km = 79.316

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