A certain enzyme, which is only found in unicorns, catalyzes the synthesis of a growth regulator that affects the properties of unicorn horns. The activity of this enzyme is dependent on the protonation state of two ionizable groups that are present in the active site: the enzyme's N-terminal amino group and an aspartate residue. Based on biochemical studies, the role of aspartate (pk4) appears to be to stabilize a positive charge of a key reaction intermediate, while the N-terminal amino group (pk, = 6.4) acts as a general acid. The active site is located in a hydrophobic pocket. %3D Construct a semi-quantitative graph (x-axis = pH and y-axis = % activity) in which you plot how the activity of this enzyme varies with pH. [HINT: Be sure to clearly plot several well-chosen points on your graph so the form of the graph is reasonable. Minimally, you must plot points for when each ionizable group is 10%, 50% and 90% ionized. Each of these points can be readily determined from the Henderson-Hasselbach equation.) %3D %3D
A certain enzyme, which is only found in unicorns, catalyzes the synthesis of a growth regulator that affects the properties of unicorn horns. The activity of this enzyme is dependent on the protonation state of two ionizable groups that are present in the active site: the enzyme's N-terminal amino group and an aspartate residue. Based on biochemical studies, the role of aspartate (pk4) appears to be to stabilize a positive charge of a key reaction intermediate, while the N-terminal amino group (pk, = 6.4) acts as a general acid. The active site is located in a hydrophobic pocket. %3D Construct a semi-quantitative graph (x-axis = pH and y-axis = % activity) in which you plot how the activity of this enzyme varies with pH. [HINT: Be sure to clearly plot several well-chosen points on your graph so the form of the graph is reasonable. Minimally, you must plot points for when each ionizable group is 10%, 50% and 90% ionized. Each of these points can be readily determined from the Henderson-Hasselbach equation.) %3D %3D
Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter6: Energy, Enzymes, And Biological Reactions
Section: Chapter Questions
Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...
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Gene expression is a process by which the instructions present in deoxyribonucleic acid (DNA) are converted into useful molecules such as proteins, and functional messenger ribonucleic (mRNA) molecules in the case of non-protein-coding genes.
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![4. A certain enzyme, which is only found in unicorns, catalyzes the synthesis of a growth regulator that affects
the properties of unicorn horns. The activity of this enzyme is dependent on the protonation state of two
ionizable groups that are present in the active site: the enzyme's N-terminal amino group and an aspartate
residue. Based on biochemical studies, the role of aspartate (pk4) appears to be to stabilize a positive
charge of a key reaction intermediate, while the N-terminal amino group (pk, = 6.4) acts as a general acid.
The active site is located in a hydrophobic pocket.
Construct a semi-quantitative graph (x-axis = pH and y-axis = % activity) in which you plot how the activity of
this enzyme varies with pH. (HINT: Be sure to clearly plot several well-chosen points on your graph so the
form of the graph is reasonable. Minimally, you must plot points for when each ionizable group is 10%, 50%
and 90% ionized. Each of these points can be readily determined from the Henderson-Hasselbach equation.]
!i!
!3!](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F8d55fdd1-c517-407c-a199-4e7fc9bcf50d%2F8e50f574-04e6-411e-a395-b9fda75cc197%2F4lb6ihj_processed.jpeg&w=3840&q=75)
Transcribed Image Text:4. A certain enzyme, which is only found in unicorns, catalyzes the synthesis of a growth regulator that affects
the properties of unicorn horns. The activity of this enzyme is dependent on the protonation state of two
ionizable groups that are present in the active site: the enzyme's N-terminal amino group and an aspartate
residue. Based on biochemical studies, the role of aspartate (pk4) appears to be to stabilize a positive
charge of a key reaction intermediate, while the N-terminal amino group (pk, = 6.4) acts as a general acid.
The active site is located in a hydrophobic pocket.
Construct a semi-quantitative graph (x-axis = pH and y-axis = % activity) in which you plot how the activity of
this enzyme varies with pH. (HINT: Be sure to clearly plot several well-chosen points on your graph so the
form of the graph is reasonable. Minimally, you must plot points for when each ionizable group is 10%, 50%
and 90% ionized. Each of these points can be readily determined from the Henderson-Hasselbach equation.]
!i!
!3!
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