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
Homework Answers
An inhibitor that binds to the active site and ends up forming a permanent covalent bond with an enzyme are irreversible inhibitor and mechanism based inhibitor
Explanation :- irreversible inhibitor and in mechanism based inhibitor bind to active site of enzyme with covalent bond and denature enzyme.
competitive inhibitor compete with substrate for enzyme binding and prevent formation of enzyme-substrate complex.
transition state analog are compound which have similar structure to enzyme-substrate complex in transition state, these analog bind to active site and inhibit reaction.
reversible inhibitor bind to enzyme active site loosely and can remove again, it not change enzyme shape or active site permanently.
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Exact question An inhibitor that binds to the active site and
ends up forming a permanent...
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...
Which of the following can bind to an enzyme at its active site? Select one: a....
Which of the following can bind to an enzyme at its active site? Select one: a. more than one correct response b. irreversible inhibitor c. reversible competitive inhibitor d. reversible noncompetitive inhibitor
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...
High concentrations of substrate overcome reversible inhibition by a transition-state analog because Question options: A. only...
High concentrations of substrate overcome reversible inhibition by a transition-state analog because Question options: A. only the substrate has the inherent ability to bind at the active-site. B. the substrate has a greater inherent affinity for the active-site. C. transition-state analogs show noncompetitive kinetics. D. the substrate will react with the transition-state analog. E. The transition-state analog is a competitive inhibitor.
BIOCHEMISTRY PALA (shown below) binds to the active site of ATCase and is an important probe...
BIOCHEMISTRY
PALA (shown below) binds to the active site of ATCase and is an
important probe molecule to study ATCase regulation. PALA acts as
_______________ type of inhibitor and acts to stabilize the
__________-state of the enzyme.
PALA{N-(phosphonasetyl)-L-aspartate.
A) uncompetitive/T
B) competitive/T
C) Uncompetitive/R
D) Competitive/R
E) Noncompetitive/R
HN Cooc Jacooo
Which statement about enzyme catalysis is false? All of the active site amino acids are next...
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
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...
You are designing a drug that inhibits a metalloprotease and is based on the structure of...
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biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
high and detecting one product at a time Question 77 The initial velocity of an enzyme...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
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...
Which of the following can bind to an enzyme at its active site? Select one: a. more than one correct response b. irreversible inhibitor c. reversible competitive inhibitor d. reversible noncompetitive inhibitor
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...
BIOCHEMISTRY
PALA (shown below) binds to the active site of ATCase and is an
important probe molecule to study ATCase regulation. PALA acts as
_______________ type of inhibitor and acts to stabilize the
__________-state of the enzyme.
PALA{N-(phosphonasetyl)-L-aspartate.
A) uncompetitive/T
B) competitive/T
C) Uncompetitive/R
D) Competitive/R
E) Noncompetitive/R
HN Cooc Jacooo
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
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...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
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