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Well, it seems my MCAT review has come full-circle. I think one of the very first questions I posted here was about lineweaver-burke, and here I am reviewing it yet again. Just wanted to make a thread because it's a little nostalgic for me. I've never put so much work into studying before, and knowing that I'll be done on Thursday is bittersweet.
y-intercept is 1/vmax, x-intercept is -1/Km.
So for competitive inhibition, the y-intercept won't change, but the x-intercept will be closer to zero (will increase).
For non-competitive inhibition, the y-intercept will be higher, since vmax decreases and thus 1/vmax increases. The x-intercept will not move because non-competitive inhibitors do not affect Km.
If the enzyme has high substrate affinity, Km is low. So, since a competitive inhibitor increases the apparent Km, it makes the enzyme less strongly attracted, or less able to bind, the substrate.
The derivation of all this, of course, comes from the Michaelis-menten equation V=Vmax*/(Km+)
Taking the inverse, 1/V=(Km +)/Vmax*, which simplifies to 1/V=(Km/Vmax*)+(/Vmax*), which further simplifies to, and takes the form of y=mx+b as 1/V=(Km/Vmax)(1/) + 1/Vmax!
y-intercept is 1/vmax, x-intercept is -1/Km.
So for competitive inhibition, the y-intercept won't change, but the x-intercept will be closer to zero (will increase).
For non-competitive inhibition, the y-intercept will be higher, since vmax decreases and thus 1/vmax increases. The x-intercept will not move because non-competitive inhibitors do not affect Km.
If the enzyme has high substrate affinity, Km is low. So, since a competitive inhibitor increases the apparent Km, it makes the enzyme less strongly attracted, or less able to bind, the substrate.
The derivation of all this, of course, comes from the Michaelis-menten equation V=Vmax*
Taking the inverse, 1/V=(Km +
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