Allosteric regulation
Japanese: アロステリック制御
A mechanism where a molecule binding to a site other than the active site regulates enzyme activity. A precise metabolic switch.
Allosteric regulation is a mechanism where a molecule binding to a site other than the active site (the allosteric site) changes the enzyme's shape and alters its activity. The term derives from Greek 'allos' meaning 'other.'
Phosphofructokinase, the rate-limiting enzyme of glycolysis, is inhibited when ATP is abundant and activated when AMP is abundant—suppressing glycolysis when energy is sufficient and promoting it when scarce. A precise cellular feedback.
Although allosteric regulation is rarely consciously considered in fermentation practice, understanding why microorganisms switch metabolism in response to their environment requires knowing this mechanism. Behind microbial 'adaptation' to temperature and pH changes lie molecular-level switches like these.