What is the correct answer? Please explain.Homework Answers
you have already marked 'b' which is the correct answer. The graph for cooperative binding is not like the one that is given. In cooperative binding the graph should be :-
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What is the correct answer? Please explain.
Consider the kinetic plot of an enzyme catalyzed reaction...
#9 quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and ...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
Question 1 2 pts How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction?...
Question 1 2 pts How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction? by decreasing the free-energy change of the reaction catalyzed by the enzyme by binding to an allosteric site, thus changing the shape of the active site of the enzyme by binding to the active site of the enzyme, thus preventing binding of the normal substrate by binding to the substrate, thus changing its shape so that it no longer binds to the active site...
12. Which of the following statements is true of enzyme catalysts? A B C To be...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
The role of an enzyme in an enzyme-catalyzed reaction is to: Select one: a. make the...
The role of an enzyme in an enzyme-catalyzed reaction is to: Select one: a. make the free-energy change for the reaction more favorable. b. ensure that the product is more stable than the substrate. c. ensure that all the substrate is converted to product. d. increase the rate at which substrate is converted into product. e. do none of the above. The focus of the online practical lesson was the enzyme chymotrypsin. The catalytic mechanism by which chymotrypsin reactions occur:...
912 Long battery life Question 5 A plot of vvSi ylelds a hyperbolic curve that plateaus...
912 Long battery life Question 5 A plot of vvSi ylelds a hyperbolic curve that plateaus as it approaches due to the air and out of 200 P Flag question Select one: a the enzymes becomes Inhibited at high substrate concentrations b. the active site is saturated with substrate. c. the enzyme's kcat increases at higher substrate concentrations o the enzyme affinity for substrate changes e. the substrate supply is becoming exhausted. Question 6 When one has to adapt to...
QUESTION 28 Among the following statements concerning the enzymes, all correct answers An apoenzyme consists of...
QUESTION 28 Among the following statements concerning the enzymes, all correct answers An apoenzyme consists of a holoenzyme and a.coenzyme Enzymes are biological catalysts that do not affect the reaction equilibrium The rate of reaction depends on the pH The catalytic site is formed of an active site and binding sites The activation energy of the uncatalyzed reaction is greater than the activation energy of the catalyzed reaction QUESTION 29 Which of the following statements are corrects? When the substrate...
Please answer all.... Thank you! 57) An enzyme binding site with a specific shape can bind...
Please answer all.... Thank you!
57) An enzyme binding site with a specific shape can bind only those having a complementary shape; thus, the shape of the protein molecule determines the specificity of the binding site the affinity of the binding site the saturation of the binding site the counding strength of the binding site Two of the above are correct. 58) A cell is what it is because of the instructions it receives concerning the types of proteins (enzymes...
4. Noncompetitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c)...
4. Noncompetitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis. 5. Which statement best describes the effect of pH upon enzyme catalyzed reactions? a) rate increases with increasing pH b) rate decreases with increasing pH c) rate increases with increasing pH until the denaturation pH is reached d) every enzyme has an optimum pH...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
Question 1 2 pts How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction? by decreasing the free-energy change of the reaction catalyzed by the enzyme by binding to an allosteric site, thus changing the shape of the active site of the enzyme by binding to the active site of the enzyme, thus preventing binding of the normal substrate by binding to the substrate, thus changing its shape so that it no longer binds to the active site...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
The role of an enzyme in an enzyme-catalyzed reaction is to: Select one: a. make the free-energy change for the reaction more favorable. b. ensure that the product is more stable than the substrate. c. ensure that all the substrate is converted to product. d. increase the rate at which substrate is converted into product. e. do none of the above. The focus of the online practical lesson was the enzyme chymotrypsin. The catalytic mechanism by which chymotrypsin reactions occur:...
912 Long battery life Question 5 A plot of vvSi ylelds a hyperbolic curve that plateaus as it approaches due to the air and out of 200 P Flag question Select one: a the enzymes becomes Inhibited at high substrate concentrations b. the active site is saturated with substrate. c. the enzyme's kcat increases at higher substrate concentrations o the enzyme affinity for substrate changes e. the substrate supply is becoming exhausted. Question 6 When one has to adapt to...
QUESTION 28 Among the following statements concerning the enzymes, all correct answers An apoenzyme consists of a holoenzyme and a.coenzyme Enzymes are biological catalysts that do not affect the reaction equilibrium The rate of reaction depends on the pH The catalytic site is formed of an active site and binding sites The activation energy of the uncatalyzed reaction is greater than the activation energy of the catalyzed reaction QUESTION 29 Which of the following statements are corrects? When the substrate...
Please answer all.... Thank you!
57) An enzyme binding site with a specific shape can bind only those having a complementary shape; thus, the shape of the protein molecule determines the specificity of the binding site the affinity of the binding site the saturation of the binding site the counding strength of the binding site Two of the above are correct. 58) A cell is what it is because of the instructions it receives concerning the types of proteins (enzymes...
4. Noncompetitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis. 5. Which statement best describes the effect of pH upon enzyme catalyzed reactions? a) rate increases with increasing pH b) rate decreases with increasing pH c) rate increases with increasing pH until the denaturation pH is reached d) every enzyme has an optimum pH...
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