This is called the induced fit model. Once the enzyme binds to the substrate, the enzyme will act as a catalyst, speed up the reaction and release the products (Biology 12, pg 50).
The rate of Enzyme activity must also be controlled, because excessive enzyme activity can cause such things as cancer and other diseases (Enzymes, 2015). There are two specific types of regulators that regulate enzymes and they are called competitive and non-competitive inhibition (Biology 12, pg 53). .
To begin with a competitive inhibitor is when an inhibitor becomes the shape of a substrate that an enzyme binds to and competes with the other substrates to bind to the enzymes active site. Once it reaches that point, it slows down the enzymatic activity. .
Non-competitive inhibition consists of two different types of inhibitors. The first one is allosteric inhibition and what it does is it binds to another part of the enzyme called the allosteric site. Furthermore it causes the enzyme to change shape so it can no longer accept and bind to substrates because its active site shape has changed. The second inhibitor for Non-competitive inhibition is called feedback inhibition. Feedback inhibition is when there are a group of enzymes a substrate must go through, changing at each one until the very last enzyme. This process goes on with other substrates until the cell thinks it is wasteful to produce that many products. Furthermore it sends an inhibitor to bind to the allosteric site of the very first enzyme in the chain and changes its active site so that the substrate cannot bind to it. Since the substrate cannot bind to the first enzyme it will not be able to bind to the other enzymes in the chain. Thus stopping the sequence of enzymes from acting as catalysts.
Turning the direction towards a specific enzyme named Catalase; it specifically acts as a catalyst with the molecule hydrogen peroxide. Hydrogen peroxide is formed as a byproduct in a lot of the chemical reactions in the human body.
