Michaelis Menten Model Lab Report

An enzyme is a biomolecule that acts as a catalyst in biochemical reactions (1). Enzymes are commonly used in many products and medications. Enzymes function by flexibly binding to active sites in substrates (reactants). This binding is weak non-covalent interactions.
The Michaelis Menten model is used to show the relationship between velocity and substrate concentration, such as in figures four and five. Vmax is the maximum rate an enzymatic reaction can have. This is calculated along with Km, the substrate concentration at half the maximum velocity and Ki, the dissociation constant. From the linear equation of the Michaelis Menten model, the Lineweaver-Burk equation is used to calculate these values (see results section, part 2 for an example).

They function by binding to the enzyme-substrate complex and are used to make drugs. There are reversible and irreversible inhibitors. The three types of reversible inhibitors include competitive, noncompetitive and uncompetitive. The type of inhibitor can be identified by the reaction Vmax, Km and Ki. In this experiment, the inhibitor used was 75 mM phenylalanine. The results in this experiment were used to study the effects of enzyme concentration, inhibitor presence and substrate concentration in a biochemical reaction. The enzyme and substrate concentrations were calculated in part 1 along with the Vmax, Km and Ki in part 2 to understand the influence of these factors on the hydrolysis reaction of 4-nitrophenylphosphate and biochemical reactions in general

By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.
In part 2, using the Michaelis-Menten kinetics of the enzyme, identified the inhibitor (75 mM phenylalanine) as an uncompetitive inhibitor. This is because Vmax and Km decrease when the inhibitor is added (7). The function of reversible, uncompetitive inhibitors is the removal of the enzyme substrate complex from circulation. This is done by the reaction creating an enzyme-substrate-inhibitor complex. An example of a common drug that is a noncompetitive inhibitor is the herbicide, Roundup. Roundup is commonly used in the genetic engineering of crops to make them more resistant to pests and can be found in much of the produce grown in the Unites States, such as corn. The function of enzymatic reactions and inhibitors is very useful knowledge because of how common the reactions are in biological