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    20.320 Exam 2 Review Problem Solutions April 20, 2006 1. No Inhibition

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    This document contains solutions to problems from a 20.320 exam on enzyme kinetics. It discusses different enzyme inhibition mechanisms including competitive, non-competitive and uncompetitive inhibition. It also provides rate equations for multi-step enzyme reactions and coupled transport and enzyme reactions. Differential equations are presented describing the change in concentration of reactants, substrates, inhibitors and complexes over time.

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    20.320 Exam 2 Review Problem Solutions April 20, 2006 1. No Inhibition

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    This document contains solutions to problems from a 20.320 exam on enzyme kinetics. It discusses different enzyme inhibition mechanisms including competitive, non-competitive and uncompetitive inhibition. It also provides rate equations for multi-step enzyme reactions and coupled transport and enzyme reactions. Differential equations are presented describing the change in concentration of reactants, substrates, inhibitors and complexes over time.

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    This document contains solutions to problems from a 20.320 exam on enzyme kinetics. It discusses different enzyme inhibition mechanisms including competitive, non-competitive and uncompetitive inhibition. It also provides rate equations for multi-step enzyme reactions and coupled transport and enzyme reactions. Differential equations are presented describing the change in concentration of reactants, substrates, inhibitors and complexes over time.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    27 views3 pages

    20.320 Exam 2 Review Problem Solutions April 20, 2006 1. No Inhibition

    Uploaded by

    Movie Scene Bank
    This document contains solutions to problems from a 20.320 exam on enzyme kinetics. It discusses different enzyme inhibition mechanisms including competitive, non-competitive and uncompetitive inhibition. It also provides rate equations for multi-step enzyme reactions and coupled transport and enzyme reactions. Differential equations are presented describing the change in concentration of reactants, substrates, inhibitors and complexes over time.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    of 3

    20.

    320 Exam 2 Review Problem Solutions April 20, 2006

    1.
    No inhibition
    vmax [ S ]
    v=
    K M + [S ]
    vmax [ S ]
    0.5vmax =
    K M + [S ]
    0.5 K M + 0.5[ S ] = [ S ]
    [S ] = K M

    Competitive
    vmax [ S ]
    v=
    ⎛ [I ] ⎞
    K M ⎜1 + ⎟ + [S ]
    ⎝ KI ⎠
    vmax [ S ]
    0.5vmax =
    ⎛ [I ] ⎞
    K M ⎜1 + ⎟ + [S ]
    ⎝ KI ⎠
    ⎛ [I ] ⎞
    0.5K M ⎜1 + ⎟ + 0.5[ S ] = [ S ]
    ⎝ KI ⎠
    ⎛ [I ] ⎞
    K M ⎜1 + ⎟ = [S ]
    ⎝ KI ⎠
    ⎛ [I ] ⎞
    ∴ K M ,CI = K M ⎜1 + ⎟
    ⎝ KI ⎠

    Non-Competitive
    ⎛ ⎞
    ⎜ v [S ] ⎟
    ⎜ max ⎟
    ⎜ 1 + [I ] ⎟
    ⎜ K I ⎟⎠
    v=⎝
    K M + [S ]
    ⎛ ⎞
    ⎜ v [S ] ⎟
    ⎜ max ⎟
    ⎜ 1 + [I ] ⎟
    ⎜ K I ⎟⎠
    0.5 max = ⎝
    v
    [ I ] KM + [S ]
    1+
    KI
    0.5 K M + 0.5[ S ] = [ S ]
    0.5 K M = 0.5[ S ]
    K M , NI = K M
    20.320 Exam 2 Review Problem Solutions April 20, 2006

    2.
    a.
    k2 k3 [ S ][ E ]0

    v=
    ( −2 + k2 + k3 )
    k
    k−1k−2 + k−1k3 + k2 k3
    + [S ]
    k1 ( k−2 + k2 + k3 )
    k−1k−2 + k−1k3 + k2 k3
    KM =
    k1 ( k−2 + k2 + k3 )
    k 2 k3
    kcat =
    ( k−2 + k2 + k3 )

    b.
    1) Assume k3 >> k2
    2) k-2 Æ 0 (irreversible)

    3. EC50 would likely be greater for a competitive inhibitor because they have to compete
    with the substrate whereas a non-competitive inhibitor does not.

    4.
    a. True
    b. False

    5.
    ρ [ R ]0
    [ L]0 
    N AV

    6.
    a.
    1) degradation
    2) recycling

    b.
    1) degradation
    2) trancytosis

    7.
    a.
    K D , AB = K D , A ⋅ KU , B = 10−4 ⋅10−3 = 10−7

    b.
    K D , AB 10−7
    KU , A = = −5 = 10−2
    K D,B 10

    c.
    K D, A 10−4
    [ A]eff = = −2 = 10−2
    KU , A 10
    20.320 Exam 2 Review Problem Solutions April 20, 2006

    d.
    1
    KU , A

    e. KD,AB increases (lower binding affinity) if linker is shorter than needed, and also
    if linker is long and very flexible. KD,AB decreases (higher binding affinity) if
    linker is rigid and "just the right length" to reach the 2nd binding site.

    8. d
    a.

    160
    140
    120
    100
    no inhibitor
    80 10^-5 inhibitor
    60
    40
    20
    0
    0 0.0005 0.001 0.0015 0.002 0.0025

    The inhibitor is a non-competitive inhibitor.

    Use Lineweaver-Burke plot to analyze Vmax, KI, and KM.

    b.
    Use non-competitive inhibitor equation.

    9.
    dRs
    = − k f Rs L + kr Cs − ker Rs + f xr k xr Ri + S R
    dt
    dCs
    = k f Rs L − kr Cs − kec Cs + f xc k xc Ci
    dt
    dRi
    = ker Rs − f xr k xr Ri − (1 − f xr ) k xr Ri
    dt
    dCi
    = kecCs − f xc k xcCi − (1 − f xc ) k xc Ci
    dt
    R0 = Ri + Rs + Ci + Cs
    Cs ρ Ci ρ
    L0 = L + +
    N AV N AV

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