For a particular chemical reaction, an inhibitor raises the $K_mathrmM$ but does not affect the $V_max $. This inhibitora. is a competitive inhibitor.b. is a noncompetitive inhibitor.c. binds to the active site of the enzyme.d. binds to an allosteric site of the enzyme.e. is a competitive inhibitor and binds to the active site of the enzyme.
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All right. So this question we were addressing a couple of complex terms. So, let's start with what we see here. This is the reaction rate of a chemical reaction. Okay. The rate the velocity over substrate concentration. Now, when we look at this this velocity here, right there where it reaches there, that's pretty much where all the enzymes are use up their well not used up but saturated being used. Okay, so that is the maximum rate that this reaction can take place. So, because of that we call that the V. Max. Okay, so it's at that velocity. All right. So the other term we have here is K. M. So what is that? That has to do not with velocity but with substrate concentration this is the substrate concentration at which the velocity as that half of the V. Max. So, if we look at the V max, this point here is about half. Okay, so we go up to the line where the reaction is and now we go down. So that point there, that is your. Kay mm. Okay. The substrate concentration at which the velocity is half of the maximum value. All right. So now for this question we also need to address inhibitors. Now there is such a thing as a competitive inhibitor and a competitive inhibitor is called competitive because it competes. What does it compete for? It competes for the active site. Now, a noncompetitive inhibitor by its name, does not bind to the active site. And often we call sites other than the active sites. We call them the Alice Terek site. Okay, so this is going to give us an idea of how things react. Okay, so a competitive inhibitor is going to inhibit the reaction. Okay, so it is going to slow down the reaction. But ultimately, ultimately what's going to happen, it's a competitive inhibitor as the substrate concentration goes up and up and up and up and up. Okay, sooner or later those substrates are going to kick off the inhibitor off the active sites. So the more substrate there is, the more inhibitor is going to get kicked off the active site and the more substrate is going to bind to the active site, so eventually you will still reach the same kmax. Okay, so that would be a competitive inhibitor. Now, a noncompetitive inhibitor, okay, again is going to inhibit, but there's a difference here, noncompetitive inhibitor is going to bind to another site. So no matter how much substrate there is, it's not going to kick it off, it's still going to be bound to it. So it's still going to continue to inhibit it. So, if you notice the noncompetitive inhibitor, V max is lower in a competitive inhibitor. V max, it is the same. Now in both those cases notice that the K. M. So the velocity is half well, here would be the K. M. Around there for the noncompetitive inhibitor, and here would be the k. M. Of the competitive inhibitor. So, in both these cases we see the K. M. Goes up. All right, so now we look at what we're looking for and agree action that raises the K. M. We know both inhibitors do that but does not affect the V. Max.
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So that would be a competitive inhibitor and we know that competitive inhibitors buying to the active site. So it would be a competitive inhibitor that binds to the active site.