For a cell to function correctly, a large number of chemical reactions need to take place. However, these reactions can often be quite slow. One way to speed up the rate of chemical reactions is by using catalysts.
Enzymes act as biological catalysts. They increase the rate of chemical reactions in living organisms without being used up or altered in the process. All metabolic reactions in the body (e.g. breaking down molecules) need enzymes.
There are two models of enzyme action:
Enzymes are large proteins, so they are made up of long chains of amino acids, which are folded into complex shapes. This means they have a unique shape.
Smaller molecules fit into an active site of enzymes. Due to the unique shape of the enzyme, the shape of the active site is complementary to its substrate molecules. Therefore, the substrate fits into the enzyme’s active site like a key in a lock. This means that in most cases, each type of enzyme can only catalyse one type of reaction.
The diagram below shows how an enzyme breaks down a substrate molecule.
However, this can also happen in reverse:
In this case, multiple substrates combine to form a single product. All the enzyme does is speed up this process. If the substrate doesn’t fit the active site of the enzyme, then the reaction will not be catalysed.
Initially, scientists thought that the substrate had to perfectly fit the active site. But we now know, that when a substrate binds to an active site, the enzyme changes shape slightly to fit the substrate perfectly.
|Lock and key||Induced fit|
|Early theory for enzyme action||The better, widely accepted theory|
|The enzyme’s active site must have a specific shape to fit the substrate||The active site can change its shape to fit the substrate|
|Enzymes are fixed structures||Enzymes are flexible structures|