A competitive inhibitor is a molecule that: Preferentially binds to an enzyme at a site other...
A competitive inhibitor is a molecule that:
- Preferentially binds to an enzyme at a site other than the active site
- Enhances the catalysis of an enzyme
- Binds to an enzyme and increases the bind strength of the substrate
- Binds to the active site and blocks the substrate
- More than one of the above.
Homework Answers
Correct answer: d. binds to the active site and blocks the substrate
A competitive inhibitor mimics the intended substrate and binds to the active site of the enzyme and thereby blocks the intended substrate from interacting with the active site of the enzyme.
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A competitive inhibitor is a molecule that:
Preferentially binds to an enzyme at a site other...
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...
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.
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...
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...
Questions #1-2 refer to Atorvastatin, which is a competitive inhibitor of the rate limiting step of...
Questions #1-2 refer to Atorvastatin, which is a competitive inhibitor of the rate limiting step of cholesterol biosynthesis. 1. What is the downstream effect of treating cells with this competitive inhibitor? A. Atorvastatin decreases the Vmax of HMG CoA synthase. B. Atorvastatin decreases the KM of HMG CoA synthase. C. Atorvastatin decreases the Vmax of HMG CoA reductase. D. Atorvastatin decreases the KM of HMG CoA reductase. E. Atorvastatin increases the KM of HMG CoA reductase. 2. Mechanistically, how does...
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...
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:...
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...
What indicates that an enzyme inhibitor binds at an allosteric site?
What indicates that an enzyme inhibitor binds at an allosteric site?a.) The inhibitor has no effect on kcat.b.) The inhibitor increases kcat.c.) The inhibitor decreases kcat.
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...
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.
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...
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...
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:...
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...
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