You undertake a research project with your favorite biology professor to analyze the behavior of an enzyme. You measure the rate of product generated as a function of how much substrate is present, setting up 6 test tubes with increasing concentrations of the substrate(s). You run three replicate experiments, one with no ATP in the tubes, one with a small amount of ATP, one with an overabundance of ATP, and take the following measurements. The amount of enzyme is the same in all tubes. Concentrations are indicated in mM (10 moles/liter) or µM (106 moles/liter). Accumulation of product in µM/sec Substrate concentration (mm) 1 2 3 4 5 10 Rate of reaction No ATP present 0.01 0 0 0.02 0 0.01 10 5 mM ATP present 1 4 7 8 8.4 8.7 10 Graph these data on the three axes provided below and answer the questions that follow. 10 5 10 Concentration of the enzymes substrate (mm) 100 mM ATP present 0.1 0.2 0.5 1 C. Could this enzyme be phosphofructokinase? Why or why not? 2 4 D. Could this enzyme be pyruvate kinase? Why or why not? A. What can you conclude about the kind of reaction this enzyme catalyzes? Explain your conclusion. 10 B. What hypothesis can you form about how this enzyme is regulated? Explain the basis of your hypothesis.
You undertake a research project with your favorite biology professor to analyze the behavior of an enzyme. You measure the rate of product generated as a function of how much substrate is present, setting up 6 test tubes with increasing concentrations of the substrate(s). You run three replicate experiments, one with no ATP in the tubes, one with a small amount of ATP, one with an overabundance of ATP, and take the following measurements. The amount of enzyme is the same in all tubes. Concentrations are indicated in mM (10 moles/liter) or µM (106 moles/liter). Accumulation of product in µM/sec Substrate concentration (mm) 1 2 3 4 5 10 Rate of reaction No ATP present 0.01 0 0 0.02 0 0.01 10 5 mM ATP present 1 4 7 8 8.4 8.7 10 Graph these data on the three axes provided below and answer the questions that follow. 10 5 10 Concentration of the enzymes substrate (mm) 100 mM ATP present 0.1 0.2 0.5 1 C. Could this enzyme be phosphofructokinase? Why or why not? 2 4 D. Could this enzyme be pyruvate kinase? Why or why not? A. What can you conclude about the kind of reaction this enzyme catalyzes? Explain your conclusion. 10 B. What hypothesis can you form about how this enzyme is regulated? Explain the basis of your hypothesis.
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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Transcribed Image Text:You undertake a research project with your favorite biology professor to analyze the behavior of an enzyme. You measure
the rate of product generated as a function of how much substrate is present, setting up 6 test tubes with increasing
concentrations of the substrate(s). You run three replicate experiments, one with no ATP in the tubes, one with a small
amount of ATP, one with an overabundance of ATP, and take the following measurements. The amount of enzyme is the
same in all tubes. Concentrations are indicated in mM (10³ moles/liter) or µM (106 moles/liter).
Accumulation of product in µM/sec
Substrate
concentration
(mm)
1
2
Rate of reaction
3
4
5
10
No ATP present
0.01
0
0
0.02
0
0.01
5 mM ATP present
1
4
7
8
8.4
8.7
Graph these data on the three axes provided below and answer the questions that follow.
10
100 mM ATP present
0.1
0.2
0.5
1
2
4
C. Could this enzyme be phosphofructokinase? Why or why not?
Concentration of the enzymes substrate (mm)
A. What can you conclude about the kind of reaction this enzyme catalyzes? Explain your conclusion.
D. Could this enzyme be pyruvate kinase? Why or why not?
10
B. What hypothesis can you form about how this enzyme is regulated? Explain the basis of your hypothesis.
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