Investigating the catalytic mechanisms of key metabolic enzymes

The fundamental idea behind enzyme catalysis is to increase the pace of a process by lowering its activation energy. Enzymes accomplish this by creating an enzyme-substrate complex by binding substrates in their active areas. This binding stabilizes the reaction's transition state through a variety of non-covalent interactions, including hydrogen bonds, ionic interactions, and Van der Waals forces. The energy barrier that needs to be broken through for the reaction to continue is lowered by this stabilization.