Alterases, also known as allosteric enzymes, are mainly characterized by their ability to undergo a change in the conformation of the enzyme molecule in the presence of a modifying substance, thereby affecting the rate of the enzymatic reaction. Alterases are generally composed of two or more subunits, which form two structural centers, one is the active center, responsible for binding to the substrate and catalyzing the reaction. The other is the allosteric center, which is responsible for binding to regulatory substances and regulating the rate of the reaction. The regulation of the reaction rate by regulatory substances can be positive or negative. When the regulatory substance binds to the enzyme and enhances the enzyme activity and speeds up the reaction rate, it is called an allosteric activator. Conversely, if it decreases the activity of the enzyme and slows down the reaction rate, it is called an allosteric inhibitor. This property of allosteric enzymes is essential for the body to regulate biochemical reactions and maintain the balance of the internal environment, and can also be a target for the treatment of certain diseases.