So in this video, we're going to take a look at the different types of inhibition: Competitive versus noncompetitive, reversible versus irreversible. So if we take a look at the first one, we're going to say we have reversible competitive inhibition. Here we have our substrate, and within the active site of our enzyme, we have the inhibitor in place. Now, here we're going to say that the inhibitor is similar in shape and size to the substrate. So it can take up the active site instead of the substrate. A great example of this is Ibuprofen. Now, what's the interaction here? Well, here this would be a non-covalent interaction between the inhibitor and the enzyme at the active site. And what is the effect? Well, the effect we can see is that it's taking up that active site position, so it's blocking it from the substrate. And how do we reverse this effect? How could we get that inhibitor to not get in the way of our substrate? Well, increasing the concentration of our substrate would help to lower the effect of this inhibitor.
Now, reversible noncompetitive. Here, we have our active site, we have our substrate, and then down here we have our inhibitor. It attached somewhere else that is not the active site. So here we're going to say that when it comes to the inhibitor, it does not resemble the substrate's shape because it's not binding to the active site where the substrate would go. A great example of this are heavy metals. Now here this is also non-covalent in terms of interaction, but now it's at the non-active site. Here, we're going to say it causes a shape change in the enzyme and in the active site. But by the enzyme, the inhibitor attaching itself to this part down here, which is not the active site, it's actually going to cause a shift or change in the shape of this active site. It changes shape so the substrate can no longer attach effectively to the enzyme. Here, we're going to say, how could we reverse this effect? Well, we have to use special types of agents. They would have to bind to the inhibitor so that they cannot bind to the non-active site and change the active site of the enzyme.
Finally, we have irreversible. Here we have our substrate, we have our enzyme, and the inhibitor has attached to the active site. Here we would say that when it comes to the inhibitor, it does not resemble the substrate's shape. In this case, we could talk about poisons and different types of venoms belonging to this type of inhibition. Now, here we're going to say we have a covalent interaction with our group within the active site. And we're going to say here that the effect is it blocks the active site. The inhibitor is attaching itself to that active site. And here the inhibition is permanent. So this can do some long-lasting damage and effects in terms of irreversible inhibition. So we've talked about the different types of inhibition, remember, competitive versus noncompetitive, reversible versus irreversible.
