Homework Answers
Ans-6- substrate binds at the active site of enzyme that is complementary to the substrate. Option B is correct
Ans-7- enzymes catalyzes the chemical reactions by decreasing the activation energy, the energy gap between the ground state and transition state of substrate. Option B is correct
Ans-8- if an inhibitor compete with the substrate for active site and binds at the active site, the phenomenon is called competitive inhibition. Option A is correct
Ans-9- since the free energy of substrate is less than the free energy of product, the reaction is endergonic because the value of delta G would be positive.
Option B is correct
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Enzyme 6. Where do substrates bind on an enzyme? A. allosteric site B. active site C....
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive 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.
a- In the induced-fit model of enzyme action, a _______ must bind to the enzyme's______ for...
a- In the induced-fit model of enzyme action, a _______ must bind to the enzyme's______ for the enzyme to perform its function. (A) catalyst; activation energy (B) product; catalytic site (C) product; active site (D) water molecule; allosteric site (E) substrate; active site b- Which of the following is CORRECT for an exergonic reaction? (A) more activation energy is needed than for an endergonic reaction (B) less activation energy is needed than for an endergonic reaction (C) products have more...
answer questions 15) An apoenzyme + cofactor(s) - a) Inhibitor b) active site c) substrate d)...
answer questions
15) An apoenzyme + cofactor(s) - a) Inhibitor b) active site c) substrate d) holoenzyme 16) Aspartate-transcarbamylase is an enveloved in a pathway that may produces molecule called Cytidine triphosphate. Cytidine triphosphate can bind to anot t o this enzyme, rendering the active site nonfunctional. This is an example of a) ATP hydrolysis b) competitive inhibition c) feedback inhibition d) allosteric activation 17) Which of the following is false regarding fermentation? a) fermentation occurs in the absence of...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is:...
1. Complete the following sentences Word bank: competitive, noncompetitive, allosteric site, oxaloacetate, active site, different from,...
1. Complete the following sentences Word bank: competitive, noncompetitive, allosteric site, oxaloacetate, active site, different from, similar to, succinate Oxaloacetate would be a reversible ______ inhibitor because the structure of oxaloacetate is ______ the structure of succinate, the substrate for the enzyme. As a _____ inhibitor, oxaloacetate would bind to the ______ of the enzyme. Increasing the concentration of _______, the substrate for the reaction, would reverse the effect of the _____ inhibitor. 2. Complete the following sentences The ______...
10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme...
10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme more tightly than the substrate. C) binds very weakly to the enzyme. D) is too unstable to isolate. E) must be almost identical to the substrate. 11. Which factor bas NOT been shown to play a role in determining the specificity of protein kinases? A) disulfide bonds near the phosphorylation site B) primary sequence at phosphorylation site C) protein quaternary structure D) protein tertiary...
7. Explain the basics of enzyme function and structure (sketch an enzyme and label the active...
7. Explain the basics of enzyme function and structure (sketch an enzyme and label the active site, allosteric site, where the substrate binds, where competitive and non-competitive inhibitors bind). Include how many different reactions can be catalyzed by an enzyme and how many times an enzyme can catalyze that reaction.
1) Substrates bind in the ____ of enzymes, which chemically alter the substrate forming a _____,...
1) Substrates bind in the ____ of enzymes, which chemically alter the substrate forming a _____, which is released by the enzyme. Select one: a. Promoter; pathway b. Quaternary structure; covalent bonds c. Substrate pocket; new substrate d. Active site; product e. Proteins; partial charge 2) Anyssa is lactose intolerant. She is unable to anabolize lactose. Select one: True False
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...
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...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive 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.
answer questions
15) An apoenzyme + cofactor(s) - a) Inhibitor b) active site c) substrate d) holoenzyme 16) Aspartate-transcarbamylase is an enveloved in a pathway that may produces molecule called Cytidine triphosphate. Cytidine triphosphate can bind to anot t o this enzyme, rendering the active site nonfunctional. This is an example of a) ATP hydrolysis b) competitive inhibition c) feedback inhibition d) allosteric activation 17) Which of the following is false regarding fermentation? a) fermentation occurs in the absence of...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is:...
10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme more tightly than the substrate. C) binds very weakly to the enzyme. D) is too unstable to isolate. E) must be almost identical to the substrate. 11. Which factor bas NOT been shown to play a role in determining the specificity of protein kinases? A) disulfide bonds near the phosphorylation site B) primary sequence at phosphorylation site C) protein quaternary structure D) protein tertiary...
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...
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...
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