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 energy than reactants
(D) products have less energy than reactants
(E) both B and C are correct
c- Enzymes:
(A) increase the rate of a chemical reaction
(B) are always stored in active form
(C) are consumed in chemical reactions
(D) raise activation energy
(E) all the above
Homework Answers
c) Enzymes increases the rate of a chemical reaction. They are not gets affected in the chemical reactions and they are need not be in thier active form.
b) Exergonic reactions are those in which energy is released during a reaction. Thses reactions have gibss energy negative that means they are spontaneous in nature hence less activation energy is needed than for an edergonic reaction and product have less energy than reactants.
a) In the induced fit model of enzyme action a substrate must bind to enezyme's active site for the enzyme to perform its function.
Hence this mechanism also reffered as lock and key mechanism.
Add Answer to:
a- In the induced-fit model of enzyme action, a _______ must
bind to the enzyme's______ for...
Enzyme 6. Where do substrates bind on an enzyme? A. allosteric site B. active site C....
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The lock and key model and the induced fit model are two models of enzyme action...
The lock and key model and the induced fit model are two models of enzyme action explaining both the specificity and the catalytic activity of enzymes. Indicate whether cach statement is part of the lock and key model, the induced fit model, or is common to both models. Lock and key model Induced fit model Common to both models Answer Bank The substrate binds to the enzyme at the active site, forming an enzyme-substrate complex The substrate binds to the...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much...
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10. A good transition-state analog: A) binds covalently to the enzyme. B) binds to the enzyme...
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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...
no explaination is needed 28) Which of the following is true for all exergonic reactions? A)...
no explaination is needed
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is meant by a "pacemaker" enzyme is an enume that catalyzes the fastest reaction in a...
is meant by a "pacemaker" enzyme is an enume that catalyzes the fastest reaction in a pathway A It is an nuryme the catalyzes the slowest reaction in a pathway c) It is in en ryme that requires a significant energy source to function D) It is an enzyme that requires a co-factor to function E) It is an enzyme that is covalently modified during the reaction process 24. What is the difference bet between the lock-and-key and the induced-fit...
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:...
All of the following apply to enzyme structure and function EXCEPT: (choose what does not apply...
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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.
Enzyme 6. Where do substrates bind on an enzyme? A. allosteric site B. active site C. receptor D. ion channel 7. Enzymes are capable of increasing the rate of a chemical reaction through which of the following means? A. changing AG from positive to negative B. reducing the activation energy C. changing the equilibrium point of the reaction D. increasing kinetic energy 8. When a molecule can occupy the same active site as the substrate, a situation called can result...
The lock and key model and the induced fit model are two models of enzyme action explaining both the specificity and the catalytic activity of enzymes. Indicate whether cach statement is part of the lock and key model, the induced fit model, or is common to both models. Lock and key model Induced fit model Common to both models Answer Bank The substrate binds to the enzyme at the active site, forming an enzyme-substrate complex The substrate binds to the...
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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...
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...
no explaination is needed
28) Which of the following is true for all exergonic reactions? A) The reaction proceeds with a net release of free energy B) The products have more total energy than the reactants. C) A net input of energy from the surroundings is required for the reactions to proceed. D) The reactions are nonspontaneous 29) When ATP releases some energy, it also releases Inorganic phosphate. What purpose does this serve (if any) in the cell? A) It...
is meant by a "pacemaker" enzyme is an enume that catalyzes the fastest reaction in a pathway A It is an nuryme the catalyzes the slowest reaction in a pathway c) It is in en ryme that requires a significant energy source to function D) It is an enzyme that requires a co-factor to function E) It is an enzyme that is covalently modified during the reaction process 24. What is the difference bet between the lock-and-key and the induced-fit...
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:...
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