Illustrated · 3 min
What Are Enzymes?
Biological molecules that change the rate of a chemical reaction are called catalysts. Enzymes are an example of catalysts.
Because they are proteins, enzymes are made up of long chains of amino acids joined together by peptide bonds.

Chain of amino acids
Image source: By National Human Genome Research Institute (NHGRI) [Public domain], via Wikimedia Commons
Enzymes almost always have names that end in -ase. If you see a molecule whose name ends in -ase, I promise you that it's an enzyme.
Examples of this include: amylase, lactase, cellulase, telomerase, and peroxidase.
Examples of the few enzymes without -ase names include: peptin, trypsin, and chrymotrypsin.
What Do Enzymes Do?
Enzymes catalyze chemical reactions. This generally means that they speed up the rate of reactions by lowering the reaction's activation energy—the energy required to get the reaction going.

Enzymes are catalysts.
Image source: By Jerry Crimson Mann, Tutmosis, Fvasconcellos (modified by expii) CC BY-SA 3.0, via Wikimedia Commons
As the image above shows, having an enzyme reduces a reaction's activation energy by quite a bit.
It's important to note that all of the reactions would still happen even if the enzymes weren't there. They'd just happen much more slowly.
Enzyme Active Site and Substrate
The reactants in an enzyme-catalyzed reaction are called substrates. Substrates must bind to enzymes before the enzymes can do their job.
Substrates bind to a specific spot on the enzyme called the active site. The shape of the active site must match the shape of the substrate, like a puzzle piece or a lock and a key.
If a substrate doesn't match an active site, then it won't bond and the enzyme can't do its job. The shapes of the substrate and active site are really important.
Once the enzyme and substrate bind, the active site changes shape slightly to fit it more closely. This is known as induced fit. Finally, we get an enzyme-substrate complex, as shown in the image below.

Image source: By Hottuna080 CC BY-SA 3.0, via Wikimedia Commons
Example of an Enzyme Reaction
Start by taking a look at the image below.

Image source: By OpenStax CC BY 3.0, via Wikimedia Commons
Let's talk about what's happening here:
- (a) There are two substrates in our reaction ( and ). They approach the enzyme.
- (b) The substrates fit into the active site and bind to the enzyme. We get our enzyme-substrate complex.
- (c) The enzyme helps the substrates bind together to form the reaction's product.
- (d) The product of the reaction is released from the enzyme. The enzyme can now be reused.
Just to mention it again (because it will come up): Enzymes are not used up or changed in chemical reactions. They can be reused over and over again.
Notice how, in our reaction above, the enzyme never changes shape. This is important because it's precisely why the enzyme can be used again.
Denaturation
Remember how we mentioned that the shape of an enzyme's active site is really important? Well, if the shape of the active site is changed or deformed, the substrates will no longer fit into it.
If substrates can't fit into the enzyme, then the enzyme can't catalyze the reaction.

Image source: By Rhannosh CC BY-SA 3.0, via Wikimedia Commons
See how the enzyme gets sort of melty looking in the last two pictures on the graph above?
This melting or deforming of the active site is called denaturation. Denaturation is primarily caused by two things:
- Extreme pH
- High temperatures
Enzyme Inhibition
There's another way to prevent an enzyme from working properly. This is called inhibition.
There are two types of inhibition:
- Competitive inhibition
- Non-competitive inhibition
Let's look at competitive inhibition first:

Image source: By Jerry Crimson Mann, TimVickers, Fvasconcellos, Retama [Public domain], via Wikimedia Commons
In competitive inhibition, something other than the substrate binds to the enzyme's active site. The thing binding to the enzyme is called the inhibitor.
Because it sits in the enzyme's active site, an inhibitor blocks the substrate from binding to the enzyme. This means that the enzyme cannot do its job.
This is called competitive inhibition because the inhibitor and the substrate compete for the active site.
Now, let's look at non-competitive inhibition:

Image source: By Jerry Crimson Mann CC BY-SA 3.0, via Wikimedia Commons
In non-competitive inhibition, an inhibitor binds to a part of the enzyme other than the active site. This bonding, as shown above, blocks the active site. This prevents the substrate from binding.
This is called non-competitive inhibition because the inhibitor and the substrate are not directly competing for the active site.
Key Vocabulary:
- Protein
- Enzyme
- Catalyst
- Activation energy
- Denaturation
- Substrate
- Active site
- Competitive inhibition
- Non-competitive inhibition





