Would the continuous assay of Alkaline phosphatase (kinetics lab) with PNPP as a substrate work if the pH of the buffer is changed from 8 to 5? Why?
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Q: Would the continuous assay of Alkaline phosphatase (kinetics lab) with PNPP as a substrate work if…
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Would the continuous assay of Alkaline phosphatase (kinetics lab) with PNPP as a substrate work if the pH of the buffer is changed from 8 to 5?
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- Explain the difference in the pKa values of the piperidinium and aziridinium ionsE53. why does alkaline phosphatase optimal at pH of 8 rather than pH 71) calculate the values of the rate constant k-1, and the value of the dissociation constant of the ES-Complex, Ks with appropriate units 2) calculate the total amount of enzyme used in the experiment and the catalytic efficiency ratio
- An enzyme reaction takes place in a 10mL solution that has a total citrate concentration of 120mM and an initial pH of 7.00. During the reaction, 0.2mmoles of acid are produced. (pKa values for citric acid: pKa1=3.15, pKa2=4.77, pKa3=6.40) a) At pH 7.00 (before the enzyme reaction occurs), determine the concentrations of the predominant forms of citrate in solution. b) calculate the pH of the solution after the enzymatic reaction has occurred.In the mechanism for cyanohydrin formation, why is HCN the acid that protonates the alkoxide ion instead of HCl?Why is NO2 a deactivator during SeAR but and activator during SnAR ?
- 4-1Based on the experimental results shown in the table, Identify whether the inhibitor acting on this enzyme is acompetitive inhibitor or a non-competitive inhibitor, and Explain the reason logically. 4-2In 4-1, the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.1. What reaction is catalyzed by the enzyme carbonic anhydrase? Which metal ion serves as a cofactor for carbonic anhydrase? Explain how this metal ion is able to assist in catalyzing the reaction. 2. In relation to enzymes, what is the difference between a cosubstrate and a prosthetic group? Give one example of each.How can distance validate non-covalent interactions? Also, please explain if the distance between c-alpha of a particular residue in an enzyme and c-alpha of its ligand are 12.4 Å, 11.7 Å, 6.5 Å, 7.6 Å, and 7.7 Å, what does that mean? What is the meaningful distance, what is the legth of hydrophobic,hydrophilic, h-bond...?
- What would be the concentration of pyrophosphate that would remain in equilibrium without hydrolyzed when, by the action of inorganic pyrophosphatase, the concentration of orthophosphate was 20 mM. (∆Gº’ pyrophosphate hydrolysis = - 30.5 kJ / mol)what happens to the pigment of egg yolk during emulsion? Explain the mechanism or the reason why the color of the mayonnaise became pale after doing emulsion (especially if properly executed)5. /Why does chalcone synthesis turn into paste if the chalcone was solid? Is the base of the mechanism catalytic?