Homework Answers
For this question, more than one answers are correct ;
1) irreversible inhibitors
2) reversible competitive inhibitors
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Which of the following can bind to an enzyme at its active site? Select one: a....
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:...
Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site...
Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site on the enzyme that is not the active site. 2. Insecticides and nerve gases act as irreversible inhibitors of nerve conduction. an enzyme needed for 3. A inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate. 4. Usually, an nhibitor forms a covalent bond with an amino acid side group within...
Classify these specific inhibitors or inhibitor characteristics according to one of three types of inhibition: reversible...
Classify these specific inhibitors or inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive Reversible noncompetitive Irreversible sulfanilamide inhibits bacterial growth inhibitor binds noncovalently at site other than active site inhibitor binds covalently at active site inhibitor structure resembles substrate structure Answer Bank inhibitor binds noncovalently at active site mercury poisons an enzyme
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...
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 ______...
A noncompetitive inhibitor has a structure that: Select one: O a. does not interfere with the...
A noncompetitive inhibitor has a structure that: Select one: O a. does not interfere with the enzyme-substrate complex formation O b. does not resemble the substrate structure c. resembles the active site of the enzyme d. can bind to the active site of the enzyme
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 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...
The active site of an enzyme ____. A. is remote form the site of substrate attachment...
The active site of an enzyme ____. A. is remote form the site of substrate attachment B. is converted to a product C. is the region where the reaction takes place D. increases the energy of reaction E. includes the entire enzyme In the lock-and-key model of enzyme actin, the enzyme active site is thought of as ___. A. a rigid, nonflexible shape that fits the substrate exactly B. an area of the enzyme that can adjust to fit the...
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:...
Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site on the enzyme that is not the active site. 2. Insecticides and nerve gases act as irreversible inhibitors of nerve conduction. an enzyme needed for 3. A inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate. 4. Usually, an nhibitor forms a covalent bond with an amino acid side group within...
Classify these specific inhibitors or inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive Reversible noncompetitive Irreversible sulfanilamide inhibits bacterial growth inhibitor binds noncovalently at site other than active site inhibitor binds covalently at active site inhibitor structure resembles substrate structure Answer Bank inhibitor binds noncovalently at active site mercury poisons an enzyme
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...
A noncompetitive inhibitor has a structure that: Select one: O a. does not interfere with the enzyme-substrate complex formation O b. does not resemble the substrate structure c. resembles the active site of the enzyme d. can bind to the active site of the enzyme
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 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 active site of an enzyme ____. A. is remote form the site of substrate attachment B. is converted to a product C. is the region where the reaction takes place D. increases the energy of reaction E. includes the entire enzyme In the lock-and-key model of enzyme actin, the enzyme active site is thought of as ___. A. a rigid, nonflexible shape that fits the substrate exactly B. an area of the enzyme that can adjust to fit the...
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