(e) [S] = 10KM 051000091 ods 26. MATHEMATICAL Determine the values of Kỵ and Vmax for the de- carboxylation of a ß-keto acid given the following data. Substrate Concentration (mol L-¹) 2.500 1.000 0.714 0.526 0.250 Velocity (mM min-¹) 0.588 0.500 0.417 0.370 0.256
(e) [S] = 10KM 051000091 ods 26. MATHEMATICAL Determine the values of Kỵ and Vmax for the de- carboxylation of a ß-keto acid given the following data. Substrate Concentration (mol L-¹) 2.500 1.000 0.714 0.526 0.250 Velocity (mM min-¹) 0.588 0.500 0.417 0.370 0.256
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Please explain question 26
![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 \( V_{\text{max}} \)?
25. **MATHEMATICAL** For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, \( V \) (as a percentage of \( V_{\text{max}} \)), observed at the following values?
(a) \([\text{S}] = K_{\text{M}}\)
(b) \([\text{S}] = 0.5K_{\text{M}}\)
(c) \([\text{S}] = 0.1K_{\text{M}}\)
(d) \([\text{S}] = 2K_{\text{M}}\)
(e) \([\text{S}] = 10K_{\text{M}}\)
26. **MATHEMATICAL** Determine the values of \( K_{\text{M}} \) and \( V_{\text{max}} \) for the decarboxylation of a β-keto acid given the following data.
| Substrate Concentration (mol L\(^{-1}\)) | Velocity (mM min\(^{-1}\)) |
|------------------------------------------|-----------------------------|
| 2.500 | 0.588 |
| 1.000 | 0.500 |
| 0.714 | 0.417 |
| 0.526 | 0.370 |
| 0.250 | 0.256 |
27. **MATHEMATICAL** The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase:
\[ \text{CO}_2 + \text{H}_2\text{O} \rightarrow \text{HCO}_3^{-} + \text{H}^{+} \]
[H. De Voe and G. B. Kistiakowsky, *J. Am. Chem. Soc.*](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F389450d8-f111-499a-811c-3e6b049ffcf7%2F155fb72f-5001-4d24-8f39-a96697dc1d92%2F7cz6tb_processed.jpeg&w=3840&q=75)
Transcribed Image Text: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 \( V_{\text{max}} \)?
25. **MATHEMATICAL** For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, \( V \) (as a percentage of \( V_{\text{max}} \)), observed at the following values?
(a) \([\text{S}] = K_{\text{M}}\)
(b) \([\text{S}] = 0.5K_{\text{M}}\)
(c) \([\text{S}] = 0.1K_{\text{M}}\)
(d) \([\text{S}] = 2K_{\text{M}}\)
(e) \([\text{S}] = 10K_{\text{M}}\)
26. **MATHEMATICAL** Determine the values of \( K_{\text{M}} \) and \( V_{\text{max}} \) for the decarboxylation of a β-keto acid given the following data.
| Substrate Concentration (mol L\(^{-1}\)) | Velocity (mM min\(^{-1}\)) |
|------------------------------------------|-----------------------------|
| 2.500 | 0.588 |
| 1.000 | 0.500 |
| 0.714 | 0.417 |
| 0.526 | 0.370 |
| 0.250 | 0.256 |
27. **MATHEMATICAL** The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase:
\[ \text{CO}_2 + \text{H}_2\text{O} \rightarrow \text{HCO}_3^{-} + \text{H}^{+} \]
[H. De Voe and G. B. Kistiakowsky, *J. Am. Chem. Soc.*
Expert Solution
Step 1: Define km and Vmax
Km and Vmax are kinetic constants that help to determine the efficiency of an enzyme.
Km is equal to [S] at Vmax/2
At Vo=Vmax/2,
Km=[S]
Vmax is the maximum velocity with which the enzyme can catalyse the reaction.
Km and Vmax can be determined accurately by using lb plot. MM plot can also be used to determine the km and Vmax but the result is not as accurate as in lb plot.
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