Answer:
By preventing the binding of substrate to active site
Explanation:
Competitive inhibitors exhibit a type of reversible inhibition. These are the substances that bind to the binding site of the substrate on the enzyme, that is the active site.
One the competitive inhibitor is bound to the active site on the enzyme, the substrate cannot bind to it and there is no enzyme-substrate complex formation. Hence, the competitive inhibitor inhibits/slow down the enzyme catalysis by occupying the active site of the enzyme and thereby not allowing the substrate to bind to the enzyme.
Answer:
a. Acetyl-CoA
Explanation:
Pyruvate is decarboxylated in the matrix of mitochondria and loses its carbon as CO2. This decarboxylation is accompanied by its oxidation as well. This process of oxidative decarboxylation of pyruvate is catalyzed by an enzyme complex. It is called the pyruvate dehydrogenase enzyme complex. NAD+ accepts the released electrons and pyruvate is converted into energy-rich acetyl CoA which in turn enters into the Kreb's cycle.
<span>Well according to my scientifical calculations i believe the correct answer is three.</span>
I'd say A. Because the only data we have is that at a 5.4 pH level, flies are not welcome.
Hope it helped!
