A high KM will result in an efficient enzyme. A. True B. False Specificity constant = Kcat/ KM kcat = Vmax [ET] A high Vmax will result in an efficient enzyme. A. True B. False Total enzyme concentration will have no effect on the efficiency of an enzyme catalysed reaction. A. True B. False
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- Which of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to workExplain as brief and simple as possible. Answers must not be more than 30 WORDS each. a. All coenzymes are cofactors, but not all cofactors are coenzymes. Explain this statement. b. How does the induced-fit model of enzyme action explain the broad specificities of some enzymes? c. In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same time? Explain your answer d. Why is penicillin toxic to bacteria but not to higher organisms? e. What is the metabolic basis for the observation that many adults cannot ingest large quantities of milk without developing gastric difficulties?1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
- Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and Km of the enzyme with no inhibitor. with inhibitor A, and with inhibitor B. [S] (uM) Vo (umol/min); w/ no inhib. Vo (umol/min); w/ inhib. A Vo (umol/min); w/ inhib. B 10 6.3 5.1 4.0 40 18.4 15.8 11.8 100 29.9 27.0 19.1 150 34.7 32.0 22.2 No inhib. Vmax= Km= Inhib. A Vmax= Km= Inhib. B Vmax= Km=Explain as brief and simple as possible. Answers must not be more than 30 WORDS each. a. How does the induced-fit model of enzyme action explain the broad specificities of some enzymes? b. In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same time? Explain your answer c. Why is penicillin toxic to bacteria but not to higher organisms?Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?
- Select all the true statements about sequential versus concerted models of allostery. a. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme b. No conformational changes occur in either model c. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding d. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formSelect all the true statements about sequential versus concerted models of allostery. Group of answer choices A. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme B. No conformational changes occur in either model C. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding D. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formPenícillin is an esxample of what type of enzyme inhíbitor? A. Competitive B. Noncompetitive C. Uncompetitive D. Irreveralble What type of Inhíbition ia observed from the ahift of the Lineweaver-Burke plot ahown in the graph below where the solid line represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhíbition D. Uncompetitive inhibition Potaszium cyanide ia a polzon which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with reapect to reduced cytochrome c. Which type of inhíbition does this represent? 9. A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhibition D. Uncompetitive inhibition Which of the following enzyme clesses catalyze reactions in which two molecules become diasociated from each other? 10. A. Kinase В. Нydrolaae C. Isomerase D. Ligase 1. Which of the…
- Which of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.What is a limitation of the Michaelis-Menten kinetics? A. Enzymes have different binding sites which were not considered by the Michaelis-Menten assumption. B. Most enzymes are multimeric with many active sites. C. Variability in enzyme concentration due to synthesis and degradation by cells were not included in the Michaelis- Menten assumption. D. Enzymes have coenzymes that are involved in catalysis. E. Active sites can bind multiple substrates.