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Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site...
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.
6) For the following statements concerning inhibition, use the answers (1 pts each) A) competitiv...
chem 103: biochem
need help with answering these questions!!!
6) For the following statements concerning inhibition, use the answers (1 pts each) A) competitive inhibition B) non-competitive C) irreversible and D) not an inhibition a) Which inhibition can be reversed by adding an excess of the substrate? b) In which inhibition does the inhibitor resemble the substrate? c) Inhibitor binds to enzyme at different site than substrate, but it can be removed. d) An example is ethanol as an antidote...
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
Exact question An inhibitor that binds to the active site and ends up forming a permanent...
Exact question An inhibitor that binds to the active site and ends up forming a permanent covalent bond with an enzyme is a (select all that apply) 1) irreversible inhibitor 2) competitive inhibitor 3) transition state analog 4) mechanism based inhibitor 5) reversible inhibitor
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...
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.
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 O sits on the active site of an enzyme blocking the subtrate inactivates...
A noncompetitive inhibitor O sits on the active site of an enzyme blocking the subtrate inactivates an enzyme by binding to the allosteric site on an enzyme and changing the shape of the active site. lowers the activation energy of the chemical reaction its involved in All of the above npu Reset Selection
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...
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...
chem 103: biochem
need help with answering these questions!!!
6) For the following statements concerning inhibition, use the answers (1 pts each) A) competitive inhibition B) non-competitive C) irreversible and D) not an inhibition a) Which inhibition can be reversed by adding an excess of the substrate? b) In which inhibition does the inhibitor resemble the substrate? c) Inhibitor binds to enzyme at different site than substrate, but it can be removed. d) An example is ethanol as an antidote...
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 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...
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 noncompetitive inhibitor O sits on the active site of an enzyme blocking the subtrate inactivates an enzyme by binding to the allosteric site on an enzyme and changing the shape of the active site. lowers the activation energy of the chemical reaction its involved in All of the above npu Reset Selection
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...
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...
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