27. MATHEMATICAL The kinetic data in the following table were ob- tained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase: CO₂ + H₂O → HCO3 + H+ [H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)]. From these data, determine KM and Vmax for the reaction. Carbon Dioxide Concentration (mmol L-¹) 1.25 2.5 5.0 20.0 1/Velocity (M¹ sec) 36 × 10³ 20 × 10³ 12 × 10³ 6 × 10³
27. MATHEMATICAL The kinetic data in the following table were ob- tained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase: CO₂ + H₂O → HCO3 + H+ [H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)]. From these data, determine KM and Vmax for the reaction. Carbon Dioxide Concentration (mmol L-¹) 1.25 2.5 5.0 20.0 1/Velocity (M¹ sec) 36 × 10³ 20 × 10³ 12 × 10³ 6 × 10³
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
Related questions
Question
Please explain question 27
![ing a solution con-
ity. Why is the de-
solution contains
plain the reaction
d rate data fit the
Findings prove the
alyst alter the stan-
have on the acti-
33AD3# 8
Formation of ATP
ct on the rate of
alyst increase the
W JLADSA CA
A? With respect
uggest how many
ed in the detailed
drogenase cata-
_D+
aviolet region of
not. Suggest an
this reaction, as-
meter capable of
eter to monitor
estion 14? Why
ng out enzymatic
induced-fit mod-
the lock-and-key
6-4 The Michaelis-Menten Approach to
Enzyme Kinetics
22. RECALL Show graphically how the reaction velocity depends
on the enzyme concentration. Can a reaction be saturated with
enzyme?
23. RECALL Define steady state, and comment on the relevance of this
concept to theories of enzyme reactivity.
24. RECALL How is the turnover number of an enzyme related to
Vmax?
25. MATHEMATICAL For an enzyme that displays Michaelis-Menten
kinetics, what is the reaction velocity, V (as a percentage of Vmax),
observed at the following values?
(a) [S] = KM
(b) [S] = 0.5 KM
gain (c) [S] = 0.1KM
(d) [S] = 2KM
Kraut
Review Exercises
(e) [S] = 10KM
26. MATHEMATICAL Determine the values of Kỵ and Vmax for the de-
carboxylation of a B-keto acid given the following data.
sris
Substrate Concentration (mol L-¹)
2.500
1.000
0.714
0.526
0.250
165
Carbon Dioxide Concentration
(mmol L ¹)
27. MATHEMATICAL The kinetic data in the following table were ob-
tained for the reaction of carbon dioxide and water to produce
bicarbonate and hydrogen ion catalyzed by carbonic anhydrase:
CO₂+ H₂O→ HCO3 + H*
1.25
2.5
5.0
20.0
Velocity (mM min-¹)
0.588
0.500
0.417
0.370
0.256
[H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)].
From these data, determine K and Vmax for the reaction.
1/Velocity
(M¹ sec)
36 × 10³
20 × 10³
12 × 10³
6 × 10³
28. MATHEMATICAL The enzyme B-methylaspartase catalyzes the](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F389450d8-f111-499a-811c-3e6b049ffcf7%2Fdbeeb859-6d14-4427-aaed-acb5d174c504%2Fwm9hcgp_processed.jpeg&w=3840&q=75)
Transcribed Image Text:ing a solution con-
ity. Why is the de-
solution contains
plain the reaction
d rate data fit the
Findings prove the
alyst alter the stan-
have on the acti-
33AD3# 8
Formation of ATP
ct on the rate of
alyst increase the
W JLADSA CA
A? With respect
uggest how many
ed in the detailed
drogenase cata-
_D+
aviolet region of
not. Suggest an
this reaction, as-
meter capable of
eter to monitor
estion 14? Why
ng out enzymatic
induced-fit mod-
the lock-and-key
6-4 The Michaelis-Menten Approach to
Enzyme Kinetics
22. RECALL Show graphically how the reaction velocity depends
on the enzyme concentration. Can a reaction be saturated with
enzyme?
23. RECALL Define steady state, and comment on the relevance of this
concept to theories of enzyme reactivity.
24. RECALL How is the turnover number of an enzyme related to
Vmax?
25. MATHEMATICAL For an enzyme that displays Michaelis-Menten
kinetics, what is the reaction velocity, V (as a percentage of Vmax),
observed at the following values?
(a) [S] = KM
(b) [S] = 0.5 KM
gain (c) [S] = 0.1KM
(d) [S] = 2KM
Kraut
Review Exercises
(e) [S] = 10KM
26. MATHEMATICAL Determine the values of Kỵ and Vmax for the de-
carboxylation of a B-keto acid given the following data.
sris
Substrate Concentration (mol L-¹)
2.500
1.000
0.714
0.526
0.250
165
Carbon Dioxide Concentration
(mmol L ¹)
27. MATHEMATICAL The kinetic data in the following table were ob-
tained for the reaction of carbon dioxide and water to produce
bicarbonate and hydrogen ion catalyzed by carbonic anhydrase:
CO₂+ H₂O→ HCO3 + H*
1.25
2.5
5.0
20.0
Velocity (mM min-¹)
0.588
0.500
0.417
0.370
0.256
[H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)].
From these data, determine K and Vmax for the reaction.
1/Velocity
(M¹ sec)
36 × 10³
20 × 10³
12 × 10³
6 × 10³
28. MATHEMATICAL The enzyme B-methylaspartase catalyzes the
Expert Solution
Step 1: Information of Lineweaver-Burk
The Lineweaver-Burk plot is used to: solve, graphically, the rate of a reaction at infinite substrate concentration.
Use this plot to calculate Michaelis–Menten constant (Km) values and Vmax.
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