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- 7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?1. The enzyme glutamate dehydrogenase is important in the breakdown of amino acids to produce NH4+. High levels of NH4+ in the body are toxic, and for this reason it is used to form urea to be excreted in the urine. a) Using the information provided, calculate the delta G knot prime and the Keq value at 298K for the oxidation of glutamate catalyzed by glutamate dehydrogenase. (Constants: R=8.3J/degree.mol, F=96.1kJ/V.mol) b) Given the reaction above, why would high levels of NH4+ be toxic? c) Given the reaction above, explain how a high concentration of gutamate inside the cell would affect energy production. Be sure to be specific.
- 2. a) Outline the general mechanism of a coenzyme B12-dependent enzyme which catalyzes the following reaction. HO H R-C-C-H ĤIÓN - H₂O HIC-H R-C-C O= H b) When R is CH3, what would the name of the enzyme be, and what would be the full EC number? Justify the first number of the EC number.5) Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number over an arrow (1, 2, 3, etc) represents an enzyme that catalyzes that reaction (so enzyme 2 catalyzes the conversion of B to C). Indicate all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway. please indicate each interaction in the format example: "X will inhibit enzyme 27".Explain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.
- A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates. It is impossible for this result to be true. OA. Adding the substrate increases the weak forces that stabilize the enzyme. OB. The high concentration of substrate forms a barrier around the hexokinase. D. Adding the substrate results in protective covalent bonding.Identify each reaction catalyzed by (a) a nucdeotidase; (b) a phosphorylase; (c) a phosphoribosyltransferase. GMP A D E Guanine Guanosine F2. Prokariotic aldolase are mediated by a Zn2+ and are inhibited by EDTA, eukaryotic aldolases though are inactivated by sodium borohydride. A) Draw out the mechanism of the eukaryotic aldolase and propose a parallel mechanism for the zinc catalyzed prokaryotic reaction. B) Propose a strategy that could be could be used to specifically inhibit prokaryotic aldolases and not eukaryotic?
- When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substratesb) Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed. HO- OH T .N -OH -OH CH₂OPO₂²-