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- The enzymatic activity of PFK1 is generally measured by set- ting up a coupled enzyme assay system whereby aldolase, triose phos- phate isomerase, and glycerol-3-phosphate dehydrogenase are added to the assay mixture. For the latter enzyme, NADH is added and its change in concentration is readily monitored at 340 nm. Write the chain of reactions catalyzed by these enzymes using structural formulas, label substrates and products, and explain why the coupled en- zyme assay system leads to oxidation of NADH. While the chain of reac- tions is similar to those in glycolysis, there is a critical difference because of the dehydrogenase enzyme. Describe how this enzyme causes the chain of reactions to differ from those in glycolysis.Pyridoxal phosphate (PLP) is a coenzyme for the enzyme ornithine aminotransferase. The enzyme was purified from cells grow in PLP = deficient media as well as from cells grown in media that contained pyridoxal phosphate. The stability of the two different enzyme preparations was then measured by incubating the enzyme at 37°C for different lengths of time and then assaying for the amount of enzyme activity remaining. The following results were obtained. (a) Why does the amount of active enzyme decrease with the time of incubation? (b) Why does the amount of enzyme from the PLP deficient cells decline more rapidly?Which statement best describes the principle behind the succinate dehydrogenase (SDH) assay used in the assay of subcellular fractions from mung bean seedlings? Question 11 options: SDH oxidized succinate to fumarate, then fumarate reduced DCPIP. Succinate is blue in colour, which is eliminated by its oxidation to fumarate by SDH. SDH produced FADH2, then FADH2 reduced DCPIP. SDH generated DCPIP, then DCPIP oxidized succinate to fumarate.
- The muscle enzyme lactate dehydrogenase catalyzes the reaction NADH and NAD+ are the reduced and oxidized forms, respectively, of the coenzyme NAD. Solutions of NADH, but not NAD+, absorb light at 340 nm. This property is used to determine the concentration of NADH in solution by measuring spectrophotometrically the amount of light absorbed at 340 nm by the solution. Explain how these properties of NADH can be used to design a quantitative assay for lactate dehydrogenase.You are studying a biochemical pathway and isolate Neurospora mutants I, II, and III.Mutant I can grow if you supplement the medium with Z.Mutant II can grow if you supplement the medium with X, Y, or Z.Mutant III can grow if you supplement the medium with X and Z, but not with Y. Draw a biochemical pathway that shows the correct order for compounds X, Y, and Z and for the enzymes that each mutant is defective for.b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.
- a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.You receive kinetic data for a transferase reaction where AX and B are substrates, while A and BX are products. You are asked to establish the reaction mechanism. Which graph will you draw first? A,B,C or D A. 1/Vo against [AXo] at different concentrations of [BXo] B. 1/[AXo] against 1/[Bo] at different concentrations of [BXo] C. 1/Vo against 1/[AXo] at different concentrations of [Bo] / D. 1/Vo against 1/[AXo] at different concentrations of [1/BXo]A yeast disaccharidase can hydrolyze sucrose and maltose according to the following table: Use Lineweaver-Burk representation to calculate the respective KMs and maximum speeds for each substrate under the conditions of the experiment. Saccharose(mM) Glucose released (µmol10 min) Maltose (mM) Glucose released (µmol10 min) 5 40 5 48 10 60 10 80 20 80 20 120 50 100 50 172 100 109 100 200
- Calculate the mass of invertase (in mg) and concentration of invertase (in mM) contained in a 25.0mL sample of yeast extract that has 3,000 total units of activity, assuming that pure invertase has a specific activity of 1,000 units/mg with a mass of 270kD.The following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and reference