Glucolate is oxidized into Glvoxylate by cytechrome C using the glycolate oxidase enzyme. The two half- reactions are shown below in their standard reduction forms. но +2 H* (aq) + 2 e Glyoxylate Glycolate
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- 1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.The rate constant for the uncatalyzed reaction of two molecules of glycine ethyl ester to form glycylglycine ethyl ester is 0.6 M- 1s - 1. In the presence ofCo2 +, the rate constant is 1.5 x 106 M- 1s - 1. What rate enhancement does the catalyst provide?
- 1. Know the structures of DNP-glycine and of the chromophore associated with cytochrome C. Low Salt Volume of blue band = 5.2 ml (Void Volume) Volume of yellow band = 2.6ml Volume of red band = 11ml High Salt Volume of blue band = 4.2 ml -> Void Volume Volume of yellow band = 5.2 Volume of red band = 1.2 2. What is the exclusion limit and the fractionation range for CM-Sephadex resin used? 3. What are the ion exchange reactions which occur when the coloured mixture is first applied to the column under low salt conditions? What exchange reactions occur upon the change of buffer from low salt to high salt concentrations? 4. What were the values for Vo and Vi for this column? Where the values for Vo and Vi the same under both conditions? 5. Explain the order in which the various components of the mixture elute under each condition in terms of their physical properties and the nature of the CMSephadex G-50 column. Would the same order be observed with a G-50 Sephadex column (i.e. no…1. What are the effects of pH and temperature to catalase? What is the optimum pH and optimum temperature for catalase? 2. Explain why the rate of reaction initially increases with increase in temperature then gradually declines as the temperature is further increased. 3. Is the rate of enzymatic reaction always directly dependent on enzyme concentration? Explain. 4. Explain the effect of substrate concentration on enzyme activity. 5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?Substrate KM (M) N-Acetylvaline ethyl ether 8.8 X 10 -2 N-Acetyltyrosine ethyl ether 6.6 X 10-4 Which substrate has the higher apparent affinity for the enzyme? Explain. Which substrate is likely to give a higher value for Vmax?
- 1. Why is the chemical logic behind the phosphorylation of glucose by hexokinase? a. So that we end the preparatory phase with 2 3-carbon compounds. b. to provide a substrate for phosphohexose isomerase. c. "Locks" Glucose in the cell. d. to decrease the ΔG of the next reaction. 2. What type of reaction does glyceraldehyde-3-phosphate dehydrogenase catalyze? a. isomerization b. group transfer c. oxidation d. dehydrationThe KM for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8 × 10−2 M, and the KM for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6 × 10−4 M. (a) Which substrate has the higher apparent affi nity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax?9. If 32p-labeled inorganic phosphate were introduced to erythrocytes undergoing glycolysis which of the following molecules would you NOT expect to detect 32p in? ** Multiple answers: Multiple answers are accepted for this question a. Fructose 1-6 bisphosphate b. 3-Phosphoglyceraldehyde c. Dihydroxyacetone phosphate d. 2-Phosphoglycerate e. 1-3 bisphosphoglycerate f. Phosphoenolpyruvate g. 3-Phosphoglycerate h. Pyruvate i. Glucose 6-Phosphate
- Using Figure 1.3 of the Introduction as an example, a) draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). HAN+-CH- COOH (CH2)4 NH°+ b) indicate the numerical pa value of each equilibrium reaction, and which ionizable group is being dissociated in each step. c) indicate the net charge of the amino acid at each step and identify the zwitterion. d) Calculate the pI of this amino acid (show the calculation). e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.5.4. If 32P labeled (radioactive phosphate) inorganic phosphate were introduced to erythrocytes undergoing glycolysis which of the following molecules would you expect to detect 32P in Glycolytic intermediates? A. Fructose 1-6 bisphosphate B. 3-Phosphoglyceraldehyde C. Dihydroxyacetone phosphate D. 2-Phosphoglycerate E. 1-3 bisphosphoglycerate F. Phosphoenolpyruvate G. 3-Phosphoglycerate H. Pyruvate I. None of the above is it E?
