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- The enzyme d-amino acid oxidase has avery high turnover number because the d-amino acids are potentially toxic. The KM for the enzyme is in the range of 1 to2 mM for the aromatic amino acids and in the range of 15 to20 mM for such amino acids as serine, alanine, and the acidicamino acids. Which of these amino acids are the preferred substrates for the enzyme?. Relation between Reaction Velocity and Substrate Concentration: MichaelisMenten Equation: At what substrate concentration would an enzyme with a kcat of 30.0s−1 and a Km of 0.0050 M operate at one-quarter of its maximum rate?What is the important values needed to calculat Km and Kcat afor an enzyme data?
- By what factor is the rate of a reaction changed if an enzyme lowers the Ea by 2.0 kJ/mol at 37°C? 32.9 times 2.2 times 10.2 times 15.1 times 7.0 timesAn enzyme whose KM is 10-4 M in the presence of a substrate concentration of 10-2 M It is capable of transforming 20% of the substrate in 10 minutes. Calculate how much substrate is had transformed in 20 minutes.From the given activity, 1.) What is the effect of temperature to the enzyme? 2.) What are some generalizations and conclusions in this activity?
- How is the maximal rate of the enzyme changed in the presence of an inhibitor?The time that is required for an enzyme to convert one substrate molecule into one product molecule is _________ A. Km. B. 1/kcat. C. 1/Km. D. kcat. Which of the following does not apply to the concerted model for subunit behavior: A. Each subunit can exist in a relaxed (R) and taut (T) conformation. B. All subunits will be in either the R or the T conformation at the same time. C. Some subunits can be in the R state while others are in the T state. D. The presence of inhibitors will lead to more of the enzyme being in the T form E. The presence of activators will lead to more of the enzyme being in the R formHow can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?
- Two curves showing the rate versus substrate concentration are shown below for an enzymecatalyzed reaction. One curve is for the reaction in the presence of substance X. The other curve is for data in the absence of substance X. Examine the curves and tell which statement below is FALSE. A. X is an activator of the enzyme. B. The enzyme exhibits non-Michaelis-Menten kinetics. C. X is likely an allosteric effector. D. X is a competitive inhibitorA4 Your enzyme is inhibited by one of the compounds depicted above. The inhibitor for your specific protein is indicated via the PDB protein code shown.On the basis of the enzyme’s structure, its substrate and mechanism of action, predict what type of enzyme inhibition ( i.e., competitive or non-competitive) may occur and justify why you think this is the case . (Up to 50 words) TYPE NOT WRITE.answer from a to D a..Which of the enzyme has greater attraction for the subtrate b..Using the graph explain you enzyme in questionC..Which enzyme has greater maximum velocity (VMax)d .why doesnt the reaction rate continue to increase with subtrate concentration?