Editing Allosteric regulation (section)

== Ortho vs. allosteric inhibitors ==

=== Orthosteric ===

# Binding Site: Orthosteric inhibitors bind directly to the enzyme's active site, where the substrate normally binds.
# Mechanism of Action: By occupying the active site, these inhibitors prevent the substrate from binding, thereby directly blocking the enzyme's catalytic activity.
# Competitive Inhibition: Most orthosteric inhibitors compete with the substrate for the active site, which means their effectiveness can be reduced if substrate concentration increases.

=== Allosteric ===

# Binding Site: Allosteric inhibitors bind to a site on the enzyme that is distinct and separate from the active site, known as the allosteric site.
# Mechanism of Action: Binding to the allosteric site induces a conformational change in the enzyme that can either reduce the affinity of the active site for the substrate or alter the enzyme's catalytic activity. This indirect interference can inhibit the enzyme's function even if the substrate is present.
# Non-Competitive Inhibition: Allosteric inhibitors often exhibit non-competitive inhibition, meaning their inhibitory effect is not dependent on the substrate concentration.