16. (20 pts). Aspartate carbamoyltransferase (ATCase) is catalyzes the first com

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16. (20 pts). Aspartate carbamoyltransferase (ATCase) is catalyzes the first committed step of pyrimidine biosynthesis. It is typically found as a catalytic tri-mer. The graph of VoVmax Vs [Substrate] for ATCase is shown below (Curve B). The graph of a standard Michaelis- Menten VoVmax is also shown (curve D). (Curves are in order with curve A on the bottom and curve D on top) 100 90 80 70 a. (6 pts) Explain the behavior of ATCase (Curve B). What is going on, why is curve B different than a standard Michaelis- Menten curve? S0 40 b. (4 pts) Curves A and C represent what happens when an allosteric inhibitor or allosteric activator are added to the reaction. Which curve corresponds to the addition of the activator, which to the inhibitor? Explain your reasoning (10 pts) When very high levels of ATP are present, the curve becomes mathematically similar to an enzyme with no allosteric interactions. Based on the graph below (the amount of enzyme is 1 mg/mL in a 1mL reaction) what are the KM, Keat, and catalytic efficiency of ATCase under these conditions? c. Asparate] uM Vo U/min 0.1 0.25 0.5 0.83 1.67 2.5 3.33 4.54

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