Regulatory enzyme. The name of the enzyme is derived from the Latin word fermentum - to ferment and the ancient Greek λεκτόρ - (lektor) - charioteer, chief in the chariot - thus denoting the main function of this enzyme: Regulatory enzymes (class A aldolases), or allosteric regulators, are represented by a number of enzymes with triple specificity. This group of enzymes includes pyridoxal phosphate-dependent monoacyltransferases and alkane dicarboxylases. All of these enzymes do not, strictly speaking, have an amino monoxide, but there is reason to call them oxidoreductases, since upon activation CoA is oxidized, although for this one of the substrates must be reduced to NAD. In addition, for many regulatory enzymes, an ambiguous explanation of the mechanisms of regulation and the attachment of allosters is possible. A large group is represented by pyrambonates: in them the regulator is “attached” to the enzyme molecule opposite its active center and activates the enzyme. In this case, the Al-egoinhibitor is associated with another allosteric molecule and in the active center there is a blocking carbon, glycine, complementary to the inactive carboxy group. First of all, allosteric regulation of the enzyme is ensured by its interaction with al-Losterol molecules, either activating or inhibiting action. Allosterone molecules bind to the protein with a subunit opposite to the active center. This "allosterol binding" changes the conformation of the protein and substrate-binding site. Similarly, for example, insulin acts on muscle tissue, promoting the transition of glucose into glycogen, has