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high and detecting one product at a time Question 77 The initial velocity of an enzyme...
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...
Which of the following is true about allosteric enyzmes? A) They typically catalyze the last reaction...
Which of the following is true about allosteric enyzmes? A) They typically catalyze the last reaction in a metabolic pathway since it is the critical step in the synthesis of the desired end product. B) They can have one subunit or several, depending on their catalytic needs. C) Their activity is often altered by a downstream product to form a feedback regulatory loop. D) They show a hyperbolic activity curve that increases with high levels of substrate. E) A and...
Question 89 Gluconeogenesis is the A) Result of amylase activity B) Formation of glycogen C) Formation...
Question 89 Gluconeogenesis is the A) Result of amylase activity B) Formation of glycogen C) Formation of starches D) Formation of glucose from simple two and three-carbon precursors Question 90 The only known regulatory mechanism for pyruvate carbora A) Activation by acetyl Co4 B) Activation by phosphorylation C) Activation by CAMP D) Activation by NADH 20 5 Question 87 Isozymes are enzymes A) From one species that catalyze the same reaction B) From different species that catalyze the same reaction...
Enzyme 6. Where do substrates bind on an enzyme? A. allosteric site B. active site C....
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...
For the following questions, multiple answers may apply. 1) Enzyme activity in cells is controlled by...
For the following questions, multiple answers may apply. 1) Enzyme activity in cells is controlled by which processes: a) covalent modifications b) modulation of expression levels c) feedback inhibition d) binding to allosteric effectors 2) Which of the following statements about the concept of “induced fit” are true (2pts): a) Substrate binding induces either global or local conformational change in the enzyme, which then brings catalytic groups into proper orientation. b) When a substrate binds to an enzyme, the enzyme...
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes t...
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes that the maximum reaction rate is proportional to the catalytic constant multiplied by the total enzyme concentration. b. It assumes that the enzyme-substrate complex concentration remains steady state. c. KM is defined as the substrate concentration at which the velocity of the reaction is maximal, so the unit is M. d. The KM is assigned to each enzyme regardless of...
Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bo...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
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...
Tarrell Lawrence: Attempt 1 Question 21 (2 points) Quodase is an enzyme that is used as...
Tarrell Lawrence: Attempt 1 Question 21 (2 points) Quodase is an enzyme that is used as a catalyst in a reaction involving quoddic acid. Aliumic acid has an almost identical shape to quoddic acid, and can bind to the active site of quodase, keeping quoddic acid from binding. In this example, aliumic acid is A) the substrate B) a coenzyme C) a competitive inhibitor D) a non-competitive inhibitor Question 22 (12 points) In nhateunthosis, the reactants are light energy, H:O,...
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:...
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...
Which of the following is true about allosteric enyzmes? A) They typically catalyze the last reaction in a metabolic pathway since it is the critical step in the synthesis of the desired end product. B) They can have one subunit or several, depending on their catalytic needs. C) Their activity is often altered by a downstream product to form a feedback regulatory loop. D) They show a hyperbolic activity curve that increases with high levels of substrate. E) A and...
Question 89 Gluconeogenesis is the A) Result of amylase activity B) Formation of glycogen C) Formation of starches D) Formation of glucose from simple two and three-carbon precursors Question 90 The only known regulatory mechanism for pyruvate carbora A) Activation by acetyl Co4 B) Activation by phosphorylation C) Activation by CAMP D) Activation by NADH 20 5 Question 87 Isozymes are enzymes A) From one species that catalyze the same reaction B) From different species that catalyze the same reaction...
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...
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes that the maximum reaction rate is proportional to the catalytic constant multiplied by the total enzyme concentration. b. It assumes that the enzyme-substrate complex concentration remains steady state. c. KM is defined as the substrate concentration at which the velocity of the reaction is maximal, so the unit is M. d. The KM is assigned to each enzyme regardless of...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
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...
Tarrell Lawrence: Attempt 1 Question 21 (2 points) Quodase is an enzyme that is used as a catalyst in a reaction involving quoddic acid. Aliumic acid has an almost identical shape to quoddic acid, and can bind to the active site of quodase, keeping quoddic acid from binding. In this example, aliumic acid is A) the substrate B) a coenzyme C) a competitive inhibitor D) a non-competitive inhibitor Question 22 (12 points) In nhateunthosis, the reactants are light energy, H:O,...
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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