2. You\'ve isolated a novel enzyme, Sadase, that cleaves the substrate Sad into
ID: 497566 • Letter: 2
Question
2. You've isolated a novel enzyme, Sadase, that cleaves the substrate Sad into the product Happy. During your study, you isolate two ligands, Schule and Lehrer. Happy produces a strong signal at 531 nm and you isolate the following data looking at the change in absorbance in 21 seconds with increasing concentrations of Sad: [Sad] V(1) (Sadase) V(2) (Sadase V(3)(Sadase Schule) Lehrer) 0.105 0.19 0.151 0.419 0.366 0.222 0.483 0.469 15 0.273 0.288 30 0.522 0.522 45 0.513 0.299 0.515 b. Comment on the possible structural similarities between the substrate and the two inhibitors. (5 points)Explanation / Answer
There´s an error in the names, the equations are correct but the names are in the opposite way.
The first thing we see is the Michaelis constant (Km)
The michaelis constant in general terms indicates de affinity between the sustract and the enzyme. If Km is high it implies that it needs a high concentration of sustract and when combined with an enzyme, it will produce the half of VMax (Vmax/2). So it means that the sustracts has a poor affinity to the enzyme.
A small Km means that it requires a small concentration of sustract to reach half of Vmax. So this means that the sustract has a rich affinity to the enzyme.
From the experiments we know that:
km for sadase+schule is 1.90485
km for sadase + lehrer is 2.6913
We can see here that the sustract has a greater affinity for sadase+schule. So for this case we can say that the sadase+schule.
Now let´s recall that effectors that enhance the protein's activity are referred to as allosteric activators, whereas those that decrease the protein's activity are called allosteric inhibitors.
So we can say that sadase+schule is a allosteric activator.
If an inhibitor is competitive, it will decrease reaction rate when there's not much substrate.
From the graphs we can see that when sadase+lehrer increase, the sadase+sad concentratio decreases (at the beginning of the graph when 1/s is close to zero which means a high concentration we can see that the rate of reaction favors sadase+sad
When sadase+schule concentration increase the sadase+sad concentration increases too.
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