Finding Michaelis-menten constant and Vmax

  1. Ok, here is the problem

    A single-substrate enzyme catalyzed reaction was investigated in the presence of 1.0 mM inhibitor as well as in the absence of inhibitor, the intial substrate concentration being constant throughout. The following results were obtained:

    ----------------intial velocity (uM/min) that is micro Molar per min
    (mM)--------=0------------ = 1.0mM
    5.0-------------161-------------111
    6.67------------194-------------141
    10.00-----------263-------------183
    20.00-----------400-------------279
    50.00-----------576-------------399

    Determine the type of inhibition exhibited by I and caluclate the values of Km apparent and Vmax apparent in the presence of 3.0mM inhibitor.

    Ok i made a Linewaver-burk plot, and it looks seems that the inhibitor is a noncompetative inhibitor because it does not change Km but it does change Vmax, but the part i am having trouble with is how to calculate Km apparent and how to calculate Vmax apparent. Will that just be the Km apparent be just the x-intercept of the Lineweaver-burk plot, and Vmax apparent be the y-intercept of the second line where 1.0mM inhibitor was used. I am not sure though because it wants these values at 3.0mM. So can some one help me out please.

    Thanks
     
  2. jcsd
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