Homework Answers
Add Answer to:
18. The following kinetic scheme that shows the Inhibitor () only binding to the enzyme-substrate (ES)...
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with...
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the descriptions and examples by classifying each statement as irreversible, competitive, or mixed inhibition. Irreversible inhibition Competitive inhibition Mixed inhibition Answer Bank the Al ion binds to acetylcholinesterase or to the acetylcholinesterase-substrate complex malonate, which resembles succinate, binds to the succinate dehydrogenase active site inhibitor may permanently modify an...
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...
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...
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 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:...
21. When you measure an enzyme reaction both without and with several concentrations of an inhibitor,...
21. When you measure an enzyme reaction both without and with several concentrations of an inhibitor, the calculated Vmay for all of the reactions remains constant. However, KM is changing with addition of the inhibitor to apparent higher values (Km apparent). What kind of inhibition is this likely to be? a. Competitive inhibition. b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition.
Which amino acids in chymotrypsin are found in the active site and are participants in substrate...
Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage? His, Ser, Asp His, Ser, Arg His, Ser Lys, Ser, Asp Where does cleavage of the peptide bond by chymotrypsin occur? On the C-terminal side of positively charged residues (lysine or). On the N-terminal side of aromatic residues (e.g. phonylalanine or tryprophase). On the C-terminal side of aromatic residues (e.g. phenylalanine or). All of the above When substrate concentration is much greater than...
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...
Which is the most inappropriate description of enzyme inhibition? Select one: a. A competitive inhibitor increases...
Which is the most inappropriate description of enzyme inhibition? Select one: a. A competitive inhibitor increases Km only. b. A noncompetitive inhibitor decreases Vmax only. c. An uncompetitive inhibitor decreases both Km and Vmax. d. All of the above e. None of the above
An uncompetitive inhibitor of an enzyme catalyzed reaction
biochemistryAn uncompetitive inhibitor of an enzyme catalyzed reaction a. binds to the ES complex b. is without effect at saturating substrate concentration. c. can actually increase reaction velocity in rare cases. d. decreases Vmax e. Binds to Es completx and lowers Vmax
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the descriptions and examples by classifying each statement as irreversible, competitive, or mixed inhibition. Irreversible inhibition Competitive inhibition Mixed inhibition Answer Bank the Al ion binds to acetylcholinesterase or to the acetylcholinesterase-substrate complex malonate, which resembles succinate, binds to the succinate dehydrogenase active site inhibitor may permanently modify an...
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...
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.
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:...
21. When you measure an enzyme reaction both without and with several concentrations of an inhibitor, the calculated Vmay for all of the reactions remains constant. However, KM is changing with addition of the inhibitor to apparent higher values (Km apparent). What kind of inhibition is this likely to be? a. Competitive inhibition. b. Uncompetitive inhibition. c. Mixed inhibition. d. Pure noncompetitive inhibition.
Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage? His, Ser, Asp His, Ser, Arg His, Ser Lys, Ser, Asp Where does cleavage of the peptide bond by chymotrypsin occur? On the C-terminal side of positively charged residues (lysine or). On the N-terminal side of aromatic residues (e.g. phonylalanine or tryprophase). On the C-terminal side of aromatic residues (e.g. phenylalanine or). All of the above When substrate concentration is much greater than...
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...
Most questions answered within 3 hours.
-
The tires of a car make 61 revolutions as the car reduces its
speed uniformly from...
asked 1 minute ago -
Peabody, Inc., sells fireworks. The company’s marketing director
developed the following cost of goods sold budget...
asked 6 minutes ago -
A signal transduction pathway includes the steps listed
below.
1. An inactive signal transduction molecule is...
asked 5 minutes ago -
1. The correlation coefficient determined for two variables has
a value of 0.89. Describe, in words,...
asked 11 minutes ago -
The following data relate to direct materials costs for
November:
Actual costs
4,700 pounds at $5.35...
asked 9 minutes ago -
Kyle, a 95.0 kg football player, leaps straight up into the air
(with no horizontal velocity)...
asked 33 minutes ago -
Which of the following is a measure of profitability?
A.
Quick (acid-test) ratio
B.
Net sales...
asked 36 minutes ago -
Find the total pressure exerted by 2 grams of ethane and 3 grams
of CO2 contained...
asked 37 minutes ago -
A fireman standing on a 5.2 m high ladder operates a water hose
with a round...
asked 33 minutes ago -
A cream formulation is studied for accelerated stability study.
Creaming was observed when formulation was tested...
asked 36 minutes ago -
A 1,150 lumen light bulb is placed 37 cm in front of a mirrored
wall, whose...
asked 46 minutes ago -
Given that z is a standard normal random variable, compute the
following probabilities (to 4 decimals)....
asked 53 minutes ago