Substrate fits exactly into the active site of the enzyme forming an enzyme/substrate complex, the reaction occurs and the products are released, the enzyme remains unchanged
Active site and substrate are not fully complementary in shape, reactive groups align and the substrate forces its way into the active site, both areas change structure slightly, the bonds in the substrate weaken and the reaction occurs at a lower activation energy
Complementary in shape to the active site of the enzyme, they prevent the formation of enzyme/substrate complexes by blocking the active site, they do not bind permanently
Bind to the enzyme away from the active site at an 'allosteric' site, this alters the shape of the active site so no enzyme/substrate complexes can be formed, some bind reversibly, others irreversibly