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    Determine Km and Vmax and determine what types of inhibition

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    Data from enzyme kinetic studies of an enzyme at specific substrate concentration. Data below also include from studies with town different inhibitors

    [S] (mM) Vo (uM/sec) Vo (uM/sec) Vo (uM/sec)
    w/o inhibitor w/inhibit A w/inhibit B

    1.3 2.5 1.17 0.62
    2.6 4.00 2.10 1.42
    6.5 6.3 4.0 2.65
    13.0 7.6 5.70 3.12
    26.0 9.0 7.20 3.58

    Determine the Km and Vmax for the enzyme not inhibited. Plot all. What types of inhibition is displayed by inhibitor A and B? Would these inhibitors have an affinity for ES or E?

    Everytime I plot this it is a curved line upside down. I do not know what I am doing wrong??? Please give me step by step. I am a very visual person.

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    Solution Preview

    [S] (mM) Vo (uM/sec) Vo (uM/sec) Vo (uM/sec)
    w/o inhibitor w/inhibit A w/inhibit B

    1.3 2.5 1.17 0.62
    2.6 4.00 2.10 1.42
    6.5 6.3 4.0 2.65
    13.0 7.6 5.70 3.12
    26.0 9.0 7.20 3.58

    The problem can be solved using the Line-Weaverburk equation:
    1/V0 = Km/Vmax (1/[S]) + 1/Vmax
    The first step is to get the 1/[S] and 1/V0 from the data above in the presence and absence of inhibitor.
    1/[S] 1/V0 (without inhibitor) 1/V0 (with inhibitor ...

    Solution Summary

    The expert determines the Km and Vmax and determines the types of inhibitions.

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