Chapter 12: Q2. (page 398)
The hypothetical elementary reaction has a rate constant of . What is the reaction velocity when the concentration of is ?
Short Answer
The reaction velocity for the hypothetical elementary reaction is 10-10Ms-1.
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Chapter 12: Q2. (page 398)
The hypothetical elementary reaction has a rate constant of . What is the reaction velocity when the concentration of is ?
The reaction velocity for the hypothetical elementary reaction is 10-10Ms-1.
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List some advantages of phosphorylation/ dephosphorylation cascade systems over simple allosteric regulation.
Determine the type of inhibition of an enzymatic reaction from the following data collected in the presence and absence of the inhibitor.
[S] (mM) | v鈧 (mM min鈦宦) | v鈧 with I present (mM min鈦宦) |
1 | 1.3 | 0.8 |
2 | 2.0 | 1.2 |
4 | 2.8 | 1.7 |
8 | 3.6 | 2.2 |
12 | 4.0 | 2.4 |
Sphingosine-1-phosphate (SIP) is important for cell survival. The synthesis of SIP from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below.
[Sphingosine] (饾泹惭) | v鈧 (mg min鈦宦) (no inhibitor) | v鈧 (mg min鈦宦) (with threo-sphingosine) |
2.5 | 32.3 | 8.5 |
3.5 | 40 | 11.5 |
5 | 50.8 | 14.6 |
10 | 72 | 25.4 |
20 | 87.7 | 43.9 |
50 | 115.4 | 70.8 |
Construct a Lineweaver-Burk plot to answer the following questions:
(a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor?
(b) What kind of an inhibitor is threo-sphingosine? Explain.
Enzyme catalyzes the reactions S to P and has a of and a of . Enzyme catalyzes the reaction and has a of and a of . When of is added to a mixture containing equivalent amounts of enzymes and , after minute which reaction product will be more abundant: P or Q?
Why might an enzyme鈥檚 substrate, transition state, and product all serve as starting points for the design of a competitive inhibitor?
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