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- In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.O D. Point of saturation 5. Idențify TRUE statement regarding the active site. * O A. A region that contains vitamins. O B. A region that binds the allosteric inhibitors. O C.A region with changing conformation. D. A region where bonds are formed between the substrate and the products. 6 Distinouish a term for a chemical reaction that has a positive AG
- 7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)3. Which of the following statements regarding enzymes and transition states is true? a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state d. formation of the transition state always assures that the reaction will proceed to product e. none of the above are true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a…3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…
- 4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.10 Which of the following is not true for an enzyme? (Circle the correct answer.) a. Increasing the temperature of an enzyme-driven reaction speeds up a reaction indefinitely. b. The reaction of an enzyme and substrate is impeded if the temperature is above or below the optimum temperature. C. Most human enzymes are more efficient near 37°C. to d. Optimum pH for most enzymes is between 6 and 8. e. Both a and d.ANN/ SUAMF 2. (a) Fig. 2.1 shows the effect of temperature on the activity of enzyme E. rate of activity/ arbitrary units 40 60 80 100 temperature/C Fig. 2.1 () State the optimum temperature for enzyme E (i1) Suggest a possible identity for enzyme E, where it is found, and its function. identity of enzyme E where it is found function on the activity of another enzyme, F
- 3 of 5 Automatic Zom Biochem LT 2. I can describe how enzymes are used as biological catalysts. 21. How does the structure of an enzyme help with its function? A. The enzyme's shape fits its substrate's shape, thus allowing the enzyme to catalyze the appropriate reaction. B. The enzyme's active site can change shape in order to match any substrates in need of a catalyst. C. The enzyme is much larger than its substrate, thus allowing the catalyzed chemical reaction to take place inside the enzyme. Use the chart to the right to answer the questions 22-23. Enzyme Effective Temperature Range ("C) Optimum pH 60 80 B. 30-NO 3.5 20-3 20-27 7. VI am finished1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false 2. These are catalyst that can be used in the monitoring and diagnosis of disease and their remarkable properties make them sensitive indicators of pathologic changes. a. enzymes b. electrolytes c. substrate d. none of these 3. ALT is stavle in serum at refrigirator or temp for up to 3 weeks, indefinitely if frozen AST has the same stability but markedly decreases with freezing a. both statement are true b. both statement are false c. first statement is true second is false d. second statement is true first statement is falseIDENTIFICATION: 1.In this model, the substrate still needs to fit into the enzyme like a key, but instead of simply fitting into the "keyhole," some type of modification is induced in the substrate, enzyme, or both. 2.Creatinine Kinase found in skeletal and heart muscle 3.Creatinine Kinase found in heart muscle 4.Creatinine Kinase found in the brain 5. To overcome an energy barrier between reactants and products, energy must be provided to get the reaction started. This energy, which is recovered as the reaction proceeds, is called: A. Potential energy B. Initiation energy C. Reaction energy D. Activation energy 6. The active site of the enzyme and substrate have complementary structures, hence they fit together as a key fits a lock. 7. TRUE or FALSE. Increase concentration of substrate, Increase enzyme action. 8. TRUE or FALSE. Decrease concentration of enzyme, Increase enzyme action.
