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a multi -subunit enzyme that has no inhibitor is most similar to the K system for an allostreic enzyme.
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Quiz Instructions Question 31 2 pts The K system for allosteric enzymes is most similar to...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in a...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in an enzyme-catalyzed biochemical reaction and propylene glycol (CH OHCH(OH)CHZ) is an inhibitor of the reaction. Would you expect propylene glycol to be a competitive or noncompetitive inhibitor? Why? Select the correct answer below: O It is likely that propylene glycol would be a competitive inhibitor because it easily binds to glycerol. O It is likely that propylene glycol would be a competitive inhibitor because it has...
Question 28 1 pts Determine the type of inhibition that has occurred in a first order...
Question 28 1 pts Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration s V 4.00 0.28 0.28 .33 0.27 0.25 0.56 0.24 0.20 0.20 0.18 0.13 0.10 0.13 0.08 O Non-competitive O Competitive O None of the above No inhibition at all...
Question 20 2 pts Which of the following anxiolytic substances is an allosteric modulator for the...
Question 20 2 pts Which of the following anxiolytic substances is an allosteric modulator for the GABA-A receptor and works by increasing the binding affinity for GABA, thus making the channel open MORE FREQUENTLY? O benzodiazepine monoamine oxidase inhibitor O barbiturate Obeta blocker O ethanol Question 21 2 pts During a panic attack, which division of the peripheral nervous system is most active? somatic O autonomic O parasympathetic O enteric O sympathetic
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 27 Which of the following statements is a true conclusion from the kinetics and equilibrium...
QUESTION 27 Which of the following statements is a true conclusion from the kinetics and equilibrium plots shown for two reaction (A and B) shown below? 100% Y х Х 0% Sec Sec A B In the given plots, Y is the reactant and X is the product Reaction B Involves a catalyst only in the forward direction Reaction A Involves a catalyst for the forward direction. Both reactions A and B are unimolecular reversible reactions QUESTION 28 Which of...
Question 1 1 pts To which of the following does a competitive inhibitor most structurally resemble?...
Question 1 1 pts To which of the following does a competitive inhibitor most structurally resemble? a coenzyme the active site the allosteric site the substrate the substrate Question 2 1 pts Glycolysis requires oxygen or another inorganic final electron acceptor to proceed. True False Question 3 1 pts During glycolysis, glucose is broken down into what? o Pyruvate oProtein ONADT oOxaloacetate
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...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
CILI ULIULIS. Question 2 The reason enzyme catalyzed reaction rates have a maximum velocity at high...
CILI ULIULIS. Question 2 The reason enzyme catalyzed reaction rates have a maximum velocity at high substrate concentrations is: Enzymes denature at high substrate concentrations. O None of the answers are correct. The enzyme active sites are saturated. O If enzymes go too fast they make mistakes. O The build-up of product limits the rate of the reaction. Question 3 TILS LICTULUGTCAICONI Question 3 4 pts For a plot of velocity vs. [S] where the maximal velocity of the uninhibited...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in an enzyme-catalyzed biochemical reaction and propylene glycol (CH OHCH(OH)CHZ) is an inhibitor of the reaction. Would you expect propylene glycol to be a competitive or noncompetitive inhibitor? Why? Select the correct answer below: O It is likely that propylene glycol would be a competitive inhibitor because it easily binds to glycerol. O It is likely that propylene glycol would be a competitive inhibitor because it has...
Question 28 1 pts Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration s V 4.00 0.28 0.28 .33 0.27 0.25 0.56 0.24 0.20 0.20 0.18 0.13 0.10 0.13 0.08 O Non-competitive O Competitive O None of the above No inhibition at all...
Question 20 2 pts Which of the following anxiolytic substances is an allosteric modulator for the GABA-A receptor and works by increasing the binding affinity for GABA, thus making the channel open MORE FREQUENTLY? O benzodiazepine monoamine oxidase inhibitor O barbiturate Obeta blocker O ethanol Question 21 2 pts During a panic attack, which division of the peripheral nervous system is most active? somatic O autonomic O parasympathetic O enteric O sympathetic
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 27 Which of the following statements is a true conclusion from the kinetics and equilibrium plots shown for two reaction (A and B) shown below? 100% Y х Х 0% Sec Sec A B In the given plots, Y is the reactant and X is the product Reaction B Involves a catalyst only in the forward direction Reaction A Involves a catalyst for the forward direction. Both reactions A and B are unimolecular reversible reactions QUESTION 28 Which of...
Question 1 1 pts To which of the following does a competitive inhibitor most structurally resemble? a coenzyme the active site the allosteric site the substrate the substrate Question 2 1 pts Glycolysis requires oxygen or another inorganic final electron acceptor to proceed. True False Question 3 1 pts During glycolysis, glucose is broken down into what? o Pyruvate oProtein ONADT oOxaloacetate
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...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
CILI ULIULIS. Question 2 The reason enzyme catalyzed reaction rates have a maximum velocity at high substrate concentrations is: Enzymes denature at high substrate concentrations. O None of the answers are correct. The enzyme active sites are saturated. O If enzymes go too fast they make mistakes. O The build-up of product limits the rate of the reaction. Question 3 TILS LICTULUGTCAICONI Question 3 4 pts For a plot of velocity vs. [S] where the maximal velocity of the uninhibited...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
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