Enzymatic catalysis

The speeding up of a process by a biological molecule known as a "enzyme" is known as enzyme catalysis. The majority of these activities, including most enzymes, involve chemical reactions. Catalysis often takes place at a specific location inside the enzyme, known as the active site. Proteins, either one protein chain or multiple chains in a multi-subunit complex, make up the majority of enzymes. Non-protein substances like metal ions or specialised chemical molecules known as cofactors are frequently included in enzymes (e.g. adenosine triphosphate). Numerous cofactors are vitamins, and their employment in the catalysis of metabolic biological processes is intimately related to their function as vitamins. It is crucial for biochemical processes in the cell to be catalysed since many, but not all, metabolically important reactions have relatively low catalytic rates. Although only the most essential enzymes operate near catalytic efficiency limitations and many enzymes are far from optimum, the optimization of such catalytic activity is one of the driving forces behind protein evolution. General acid-base catalysis, orbital steering, entropic restriction, orientation effects (such as lock-and-key catalysis), and motional effects involving protein dynamics are important aspects of enzyme catalysis. Although enzyme catalysis mechanisms differ, they are all fundamentally comparable to other forms of chemical catalysis in that lowering the energy barrier(s) separating the reactants from the products—or substrates—is essential. The proportion of reactant molecules that can get past this obstacle and create the product increases when activation energy (Ea) is reduced.