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But the non competitive inhibition, doesn't the michaelis graph shows a different Km since Vmax is reduced and Km is 1/2 Vmax so the point corresponding to Km is not the same. Anyone can explain to me
Why does the competitive inhibitor line start from Control's Km? Shouldn't it start from same place as normal but slope shifted to the right, but still "reaching" Vmax?
Adding more substrate increases the Km cause there will be more substrate present to saturate the enzyme so the enzyme will have less affinity for the substrate; remember that Vmax increases when the number of enzymes increases. Hope this helps!
