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Michaelis Menten Model Lab Report

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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). …show more content…

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 …show more content…

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

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ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.

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The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably

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The common sites for phosphorylation like protein of amino acid threonine and serine. Many enzymes that involved in intracellular signaling pathways are control by these phosphorylation reactions. The enzyme activity can be activate or inhibit depends on the addition of phosphate groups that cause the conformational change in enzymes. At certain time, the phosphate groups will eliminate from the enzymes by protein phosphatases in that way reversing the effect on enzymatic

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Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).

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As per table 3. there is a pattern with the enzyme concentration going from 100% to 0%, at 100% the rate of O2 production is at its highest being 7.79mL/min while at 0% the rate of O2 production is at its lowest being 0mL/min. In Table 4. the substrate concentration has the same pattern as the enzyme concentration, at the highest concentration being 3% the rate of O2 production is 7.58mL/min and at the lowest

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Koshland proposed induced fit hypothesis in 1959. The active sites of these enzymes have shapes that are complementary to that of the substrate only after the substrate is bound. Such enzyme-substrate interaction are described by induced fit model. The advantages of the induced fit mechanism arise due to the stabilizing effect of strong enzyme binding. There are two different mechanisms of substrate binding: uniform binding, which has strong substrate binding, and differential binding, which has strong transition state binding.

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ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.

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3.1. Optimization of the reaction conditions The experimental parameters affecting the development and stability of the reaction product between the drug and the reagent were investigated and optimized. Each parameter was changed individually while the others were kept constant. These parameters include; pH, buffer (type & volume), concentration of NBD-Cl, reaction and stability time, temperature, acidification and diluting solvent.

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It was well known that the collisions between enzyme and substrate molecules increased with an increase in temperature that result in an increase in reaction rate and thus the conversion. It was observed that with an increase in enzyme loading from 1-2% (w/w) increase in percentage conversion. Usually, an increase in enzyme loading increases the number of active sites and therefore more substrate molecules converted into products. The highest conversion could be attained when the enzyme loading was taken to be 2% in combination with the temperature 50 ˚C.

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Additionally, there exists three domains of the enzyme namely C- terminal catalytic domain, an N- terminal regulatory domain and a tetramerization domain. Tetrahydrobiopterin (BH4) acts as a cofactor for the enzyme activity. Hence, the regulatory action by PAH enzyme involves activation by the presence of the amino acid phenylalanine, inhibition by the cofactor Tetrahydrobiopterin (BH4) and activation of the enzyme by phosphorylation. Cyclic adenosine monophosphate (cAMP) – dependent protein kinase helps in the phosphorylation of the amino acid serine that is present on the 16 position of the regulatory domain of the enzyme. This in turn helps in maintaining the activity of the enzyme by reducing the concentration of the phenylalanine

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