Consider the reaction: H H SCOA a. What kind of reaction is being performed here? b. What enzyme performs this reaction? c. What cofactors, if any, are required for this reaction? H H 0=U SCOA
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- Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…4. Consider the reaction: OH CH H3C O C H₂ a. What kind of reaction is being performed here? H3C C H₂ b. What enzyme performs this reaction? c. What cofactors, if any, are required for this reaction?7. Consider the reaction: H3CC-CH₂-C—S-ACP H3C OH b. What enzyme performs this reaction? C-CH₂-C—S-ACP a. What kind of reaction is being performed here? c. What cofactors, if any, are required for this reaction?
- 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)1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Seriosa. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What kind of reaction occurred when 1 was converted to 2? d. What general kind of enzyme might you expect to perform this reaction? e. What cofactor, if any, would be required for this reaction?
- 3. Draw a properly-labeled reaction progress diagram with two lines: one line for the enzyme-catalyzed reaction, and one line for the enzyme-uncatalyzed reaction. The simplified expression for the reaction is S→ P. Assume this reaction is thermodynamically favorable. Show all appropriate species for the enzymatic reaction. Then, answer these questions: A) Are AG and AG# the same thing? B) Which of these properties is related to reaction velocity (k), and what equation describes that relationship? C) Finally, exactly how do enzymes speed up reaction rates? In your answer, please provide both a thermodynamic argument AND a structural argument.4.Pepsin is the proteolytic enzyme of gastric juice. The active form of this enzyme is formed from pepsinogen under HCL action.Optimum of enzyme action: pH = 1.5, t = 37°. Describe the properties of this enzyme. For this:1)Name and explain the mechanism of this enzyme activation.2)Draw the plot and explain the effects of pH and t on the reaction velocity.3) Explain how changes the velocity of this reaction in patients suffering from hypoacidie gastritis.Give a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativit
- 3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?3. Consider the reaction: H3C-(CH₂) H H C—C—C—SCOA HH H₂C-(CH₂) a. What kind of reaction is being performed here? b. What enzyme performs this reaction? -C—C—C—SCOA H H c. What cofactors, if any, are required for this reaction?1. Calculate the pH of a 0.05 M solution of HCl. 2. Calculate the pH of a 0.1 M solution of NaOH. 3. Calculate the pH of an acetic acid solution in which [CH3COO - ] = 0.037 M and [CH3COOH] = 0.044 M. (pKa = 4.76) 4. You are conducting a biochemical experiment with an enzyme that has optimal activity at pH = 10.00. You decide to use carbonate (pKa1 = 6.38, pKa2 = 10.30) as the buffer to keep the pH stable throughout the enzymatic reaction. (Recall that the formula for carbonic acid is H2CO3.) You prepare a 0.5 M solution of carbonate buffer at pH = 10.00. Calculate the concentrations of the major carbonate species in your solution. 5. Calculate the pH of the buffer solution in which [H3PO4] = 0.038 M and [H2PO4 - ] = 0.046 M (pKa1 = 2.12, pKa2 = 7.21, pKa3 = 12.32). 6. Add 5.0 mL of 0.1 M NaOH to 80 mL of buffer from question 5 and calculate the pH.