What is a Lineweaver-Burke plot?
A. It is simply a different way to plot the data found in a Michaelis-Menten-type experiment. It should give you a straight line instead of a curve. You should know that the slope of the line is proportional to the Km. The steeper the slope, the slower the enzyme is turning over at a given concentration. If you add an inhibitor of the reaction, the slope increases. If it is a competitive inhibitor, the y-intercept will remain constant (1/Vmax). If it is a non-competitive inhibitor the x-intercept will remain constant (-1/Km). 12. What’s the difference between a competitive and non-competitive inhibitor? A: Competitive: Vmax constant, Km changes; Non-competitive: Km constant, Vmax changes. A competitive inhibitor competes with the substrate for binding to the active site. If the inhibitor is present in the active site, the substrate cannot bind. By adding A LOT of substrate, the inhibitor can no longer effectively compete (since it is outnumbered), so the original rate (Vmax) of turnove
