Editing Binding site (section)

=== Catalysis ===
[[File:ActivationEnergyInt.svg|thumb|[[Activation energy]] is decreased in the presence of an enzyme to catalyze the reaction.]]
Enzymes incur catalysis by binding more strongly to [[transition state]]s than substrates and products. At the catalytic binding site, several different interactions may act upon the substrate. These range from electric catalysis, acid and base catalysis, covalent catalysis, and metal ion catalysis.<ref name="Wilson_2010" /> These interactions decrease the activation energy of a chemical reaction by providing favorable interactions to stabilize the high energy molecule. Enzyme binding allows for closer proximity and exclusion of substances irrelevant to the reaction. Side reactions are also discouraged by this specific binding.<ref name=":52">{{Cite book | vauthors = Dobson JA, Gerrard AJ, Pratt JA |title=Foundations of chemical biology |date=2008|publisher=Oxford University Press|isbn=9780199248995|oclc=487962823}}</ref><ref name="Wilson_2010" />

Types of enzymes that can perform these actions include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.<ref>{{cite book | vauthors = Azzaroni O, Szleifer I |date=2017-12-04|title=Polymer and Biopolymer Brushes |doi=10.1002/9781119455042 | isbn = 978-1-119-45501-1 }}</ref>

For instance, the transferase hexokinase catalyzes the phosphorylation of glucose to make glucose-6-phosphate. Active site residues of hexokinase allow for stabilization of the glucose molecule in the active site and spur the onset of an alternative pathway of favorable interactions, decreasing the activation energy.<ref>{{Cite book|title=Dictionary of Food Science and Technology|publisher=International Food Information Service|year=2009|isbn=978-1-4051-8740-4|edition=2nd}}</ref>