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    I know the effect of a competitive inhibitor on the kinetics is to increase the value of Km and thus a higher conc of substrate is needed for full saturation of the enzyme, but what is the effect on the kinetics using a NON competitive inhibitor?
    I am aware of the graph,and how it doesn't reach Vmax but can someone explain the Km aspect?
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    (Original post by dinesh)
    I know the effect of a competitive inhibitor on the kinetics is to increase the value of Km and thus a higher conc of substrate is needed for full saturation of the enzyme, but what is the effect on the kinetics using a NON competitive inhibitor?
    I am aware of the graph,and how it doesn't reach Vmax but can someone explain the Km aspect?
    For noncompetitive inhibitors the Km remains the same.

    (the Km for the green and pink lines are the same)


    taken from here: http://users.rcn.com/jkimball.ma.ult...eKinetics.html
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    Yes - for non-competitive inhibitors, Vmax decreases and Km remains the same (ie binding of the substrate isn't affected, but the catalytic activity of the enzyme is reduced).

    NB - make sure you call in non-competitive. There is another class of inhibitors that you don't need to know about called uncompetitive, so make sure you get the wording right in the exam!
 
 
 
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