00:01
So basically this question is asking us what is true of competitive inhibition.
00:06
So let's look at the background of inhibition.
00:10
So if we have an enzyme here, there's an active site where normally the substrate would bind, but in this case we have an inhibitor.
00:22
So this is going to be a competitive inhibitor, which is going to try to bind at the active site instead of the substrate.
00:29
So the enzyme can bind the inhibitor or can compete with the substrate.
00:34
Basically the substrate here and the enzyme are competing for the same exact active site.
00:39
And notice how there's only one thing binding at the active site here, either the inhibitor or, oops, the inhibitor or the substrate.
00:52
So if we look at the typical graph, we see, so in a normal enzyme substrate reaction, we have this type of curve here where the vma.
01:03
So this is the initial rate of reaction against the substrate concentration.
01:09
So we have a km, which is half the substrate concentration at half of the vmax.
01:15
So km is going to be on this line here, and your vmax is going to be on this line.
01:20
And then if we put a competitive inhibitor in, you'll have this line over here.
01:27
So if you notice the km is shifted, right? so it moves over, so it's higher.
01:32
But it does reach the same vmax.
01:36
So vmax is the same, but km is changing.
01:44
It's not the same...