Editing Binding site (section)

=== Inhibition ===
Protein inhibition by inhibitor binding may induce obstruction in pathway regulation, homeostatic regulation and physiological function.

[[Competitive inhibition|Competitive inhibitors]] compete with substrate to bind to free enzymes at active sites and thus impede the production of the enzyme-substrate complex upon binding. For example, carbon monoxide poisoning is caused by the competitive binding of carbon monoxide as opposed to oxygen in hemoglobin.

[[Uncompetitive inhibitor]]s, alternatively, bind concurrently with substrate at active sites. Upon binding to an enzyme substrate (ES) complex, an enzyme substrate inhibitor (ESI) complex is formed. Similar to competitive inhibitors, the rate at product formation is decreased also.<ref name="Hardin_2013" />

Lastly, mixed inhibitors are able to bind to both the free enzyme and the enzyme-substrate complex. However, in contrast to competitive and uncompetitive inhibitors, mixed inhibitors bind to the allosteric site. Allosteric binding induces conformational changes that may increase the protein's affinity for substrate. This phenomenon is called positive modulation. Conversely, allosteric binding that decreases the protein's affinity for substrate is negative modulation.<ref>{{cite book | vauthors = Clarke KG |date=2013 |title=Bioprocess engineering |publisher=Woodhead Publishing |pages=79–84 |doi=10.1533/9781782421689 |isbn=978-1-78242-167-2 }}</ref>