Can someone elaborate on competitive and noncompetitive enzyme inhibition. Include either Michaelis Menten or Lineweaver-Burk plots for each. Label the exes fully and indicate what happens to Km and Vmax. Please, thank you.
These are Lineweaver Burk plots.
Competitive inhibitor - competitive inhibitor is similar in shape and size to the substrate of the enzyme and binds to the active site of the enzyme so that the substrate cannot bind to it.
Noncompetitive (uncompetitve) inhibitor - binds to the site other than active site of the enzyme, it is not similar in shape and size to the substrate, but its binding to the enzyme changes the conformation of active site so that substrate cannot bind to it.
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