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22. Structurally illustrate enzyme-substrate complex formation with respect to an allosterle site binding.
22. Structurally illustrate enzyme-substrate complex formation with respect to an allosterle site binding
22. Structurally illustrate enzyme-substrate complex formation with respect to an allosterle site binding
Enzyme E bind to substrate S to form ES complex leading to product formation. However, the ES com...
Enzyme E bind to substrate S to form ES complex leading to product formation. However, the ES complex also undergoes suicidal inactivation that would result in the loss of the total enzyme activity. In addition, after the binding of S to E there exposes another binding site in E for uncompetitive inhibitor I. The ESI complex does not have the capacity to form product and would not undergo inactivation. The equilibriums, reactions and the kinetic parameters involved can be represented...
19. A molecule that is structurally similar to the substrate for an enzyme will probably be...
19. A molecule that is structurally similar to the substrate for an enzyme will probably be a: 2. Competitive inhibitor b. Cofactor c. Regulator d. Noncompetitive inhibitor
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...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42....
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
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...
Enzyme labeling can be used to map the structure of the active site of an enzyme...
Enzyme labeling can be used to map the structure of the active site of an enzyme using an affinity label, a molecule that is structurally similar to the substrate. Which of the following statements about enzyme labeling is true?
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work...
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work best a the substrate changes its conformation to fit the active site b. the active site changes its conformation to fit the substrate c. the active site is rigid and the substrate must fit exactly d. the substrate binds only to part of the active site In the induced-fit model of substrate binding a. 57. the substrate changes its conformation to fit the active...
18. The following kinetic scheme that shows the Inhibitor () only binding to the enzyme-substrate (ES)...
18. The following kinetic scheme that shows the Inhibitor () only binding to the enzyme-substrate (ES) complex is typic of what type of enzyme inhibition? E + SEES -E + PSN ESI no reaction A) Irreversible B) Competitive C) Noncompetitive D) Uncompetitive or acetylcholinesterase 19. DIFP acts as an inhibitor of the enzyme chymotrypsin. A) Irreversible B) Competitive C) Uncompetitive D) Mixed
The following occur in enzyme-catalyzed reactions except A. The substrate is transformed at the active site...
The following occur in enzyme-catalyzed reactions except A. The substrate is transformed at the active site B. The enzyme does not undergo any change change C. Enzyme-substrate complex is formed O D. Activation energy of the reaction is increased O E. Activation energy is lowered QUESTION 34 bonds In the alpha helical structure of the DNA, the base G pairs with the base c by A. 3 hydrogen B. 3 covalent C. 2 covalent D.3 amide E. 2 hydrogen
22. Structurally illustrate enzyme-substrate complex formation with respect to an allosterle site binding
Enzyme E bind to substrate S to form ES complex leading to product formation. However, the ES complex also undergoes suicidal inactivation that would result in the loss of the total enzyme activity. In addition, after the binding of S to E there exposes another binding site in E for uncompetitive inhibitor I. The ESI complex does not have the capacity to form product and would not undergo inactivation. The equilibriums, reactions and the kinetic parameters involved can be represented...
19. A molecule that is structurally similar to the substrate for an enzyme will probably be a: 2. Competitive inhibitor b. Cofactor c. Regulator d. Noncompetitive inhibitor
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...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
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...
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work best a the substrate changes its conformation to fit the active site b. the active site changes its conformation to fit the substrate c. the active site is rigid and the substrate must fit exactly d. the substrate binds only to part of the active site In the induced-fit model of substrate binding a. 57. the substrate changes its conformation to fit the active...
18. The following kinetic scheme that shows the Inhibitor () only binding to the enzyme-substrate (ES) complex is typic of what type of enzyme inhibition? E + SEES -E + PSN ESI no reaction A) Irreversible B) Competitive C) Noncompetitive D) Uncompetitive or acetylcholinesterase 19. DIFP acts as an inhibitor of the enzyme chymotrypsin. A) Irreversible B) Competitive C) Uncompetitive D) Mixed
The following occur in enzyme-catalyzed reactions except A. The substrate is transformed at the active site B. The enzyme does not undergo any change change C. Enzyme-substrate complex is formed O D. Activation energy of the reaction is increased O E. Activation energy is lowered QUESTION 34 bonds In the alpha helical structure of the DNA, the base G pairs with the base c by A. 3 hydrogen B. 3 covalent C. 2 covalent D.3 amide E. 2 hydrogen
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