) of a reaction. Instead, they change the reaction pathway to lower the activation energy ( Eacap E sub a
Inhibitors are molecules that interact with enzymes to reduce their catalytic rate. They are essential tools for mapping metabolic pathways and serve as the foundation for modern pharmacology. Inhibition Type Binding Site Vmaxcap V sub m a x end-sub Kmcap K sub m Lineweaver-Burk Intersection Active Site Intersects at the Y-axis Non-competitive Allosteric Site Intersects at the X-axis Uncompetitive Enzyme-Substrate Complex Parallel lines Reversible vs. Irreversible Inhibition ) of a reaction
Taking the reciprocal of the Michaelis-Menten equation yields a straight line ( Inhibition Type Binding Site Vmaxcap V sub m
is an inverse measure of the enzyme's affinity for its substrate; a low Kmcap K sub m ) of a reaction. Instead
Enzymes can increase reaction rates by factors of 10610 to the sixth power 101210 to the 12th power compared to uncatalyzed reactions.