1-In the first experiment, the researchers use a total enzyme concentration ([Et]) of 4 nM. They find that the happyase has a Vmax of 1.6 µs-1 in these conditions. Calculate the k2 of happyase based on this finding. Show your work and include appropriate units. 2-In another experiment, with [Et]=1 nM and [HAPPY]=30 µM, the researchers find that V0 = 300 nM.s-1. Calculate the Km of happyase for its substrate HAPPY based on this finding. Show your work and include appropriate units. 3-Further research shows that the purified happyase enzyme used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. After the careful removal of ANGER, the measured Vmax is increased to 4.8 µM.s-1, and the calculated Km becomes equal to 15 µM. Compare these values of Vmax and Km to that obtained in the experiments described in 1 and 2. To which category of reversible inhibitor ANGER belongs to? Explain.
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
A research group discovers a new enzyme they decide to name happyase. This enzyme has a Michaelian behavior and catalyzes the
HAPPY ↔ SAD
The researchers begin to characterize the enzyme.
1-In the first experiment, the researchers use a total enzyme concentration ([Et]) of 4 nM. They find that the happyase has a Vmax of 1.6 µs-1 in these conditions. Calculate the k2 of happyase based on this finding. Show your work and include appropriate units.
2-In another experiment, with [Et]=1 nM and [HAPPY]=30 µM, the researchers find that V0 = 300 nM.s-1. Calculate the Km of happyase for its substrate HAPPY based on this finding. Show your work and include appropriate units.
3-Further research shows that the purified happyase enzyme used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. After the careful removal of ANGER, the measured Vmax is increased to 4.8 µM.s-1, and the calculated Km becomes equal to 15 µM. Compare these values of Vmax and Km to that obtained in the experiments described in 1 and 2. To which category of reversible inhibitor ANGER belongs to? Explain.
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