How are Enzymes Controlled?
How are enzymes controlled?
Enzymes are known to be very powerful catalysts. To control the metabolism, the following treatments are to be followed by organism:
- Controlling the amounts of an enzyme made
- Organizing the location of the enzymes in each cell/ the whole organism
- Controlling the catalytic power of the enzyme molecules after they are made
Our genes are known to carry the code, which makes enzymes. Some of the molecules may contain the ability to switch the genes on/off to regulate the amount of a particular enzyme which a cell makes. For example, a gene might be induced (switched on) by the substrate for the enzyme that it makes.
The genetic regulation is a very simple process. Some of the enzymes are created in an inactive form. These are activated right after they are in the required position. Some of the digestive proenzymes are produced in the pancreas. They are not activated if they are not released into the duodenum.
There are sections surrounded by membrane inside every cell. Specific cells contain enzymes that can be packed away here. The cells can regulate the reaction rate which involves the regulation of the movements of substrate molecules through the membrane.
Hormones are often used by the organisms to carry messages from parts of one organism to another. Some of these lock on to the receptors in the cell membranes and begin a series of changes which triggers the activation of enzymes inside the cell. The adrenaline follows the same route.
The catalytic activities of an enzyme can be controlled(increased/decreased) by small molecules. This is done through tying to its molecules. The inhibitor ties the active site and blocks the entry of substrate. Both the inhibitor and the substrate have comparable structures. The penicillin prevents the active sties of enzymes while aiding the construction of cell walls of bacteria.
Smaller molecules may bind quite far from the active site and activate/inhibit the change of conformation of the enzyme. This is known as the allosteric effect.
The enzyme activities may be controlled and by monitoring the availability of cofactors which are inversely bound to the enzyme or the substrate.