2. Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Еquation (a) At what substrate concentration will an enzyme having a kcat of 30 s' and a KM of 0.005 M show one-quarter of its maximum rate? (b) Determine the fraction of Vmax that would be found in each case when [S] = ½KM, 2KM, and 10KM.
2. Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Еquation (a) At what substrate concentration will an enzyme having a kcat of 30 s' and a KM of 0.005 M show one-quarter of its maximum rate? (b) Determine the fraction of Vmax that would be found in each case when [S] = ½KM, 2KM, and 10KM.
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
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![2. Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten
Equation
(a) At what substrate concentration will an enzyme having a kcat of 30 s² and a KM of
0.005 M show one-quarter of its maximum rate?
(b) Determine the fraction of Vmax that would be found in each case when
[S] = ½KM, 2KM, and 10KM.
3. Protection of Enzyme Against Denaturation by Heat
When enzyme solutíons are heated, there is a progressive loss of catalytic activity with time.
This loss is the result of the unfolding of the native enzyme molecule to a randomly coiled
conformation, because of its increased thermal energy. ´A solution of the enzyme hexokinase
incubated at 45 °C, lost 50% of its activity in 12 mins, but when hexokinase was incubated at
45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its
activity. Explain why thermal denaturation of hexokinase was retarded in the presence of one of
its substrates.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F85793e9a-8859-44de-af1b-868e70709835%2Ff9fc4d27-7bd3-4369-b4ef-04575c160505%2Fgjehkdr_processed.jpeg&w=3840&q=75)
Transcribed Image Text:2. Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten
Equation
(a) At what substrate concentration will an enzyme having a kcat of 30 s² and a KM of
0.005 M show one-quarter of its maximum rate?
(b) Determine the fraction of Vmax that would be found in each case when
[S] = ½KM, 2KM, and 10KM.
3. Protection of Enzyme Against Denaturation by Heat
When enzyme solutíons are heated, there is a progressive loss of catalytic activity with time.
This loss is the result of the unfolding of the native enzyme molecule to a randomly coiled
conformation, because of its increased thermal energy. ´A solution of the enzyme hexokinase
incubated at 45 °C, lost 50% of its activity in 12 mins, but when hexokinase was incubated at
45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its
activity. Explain why thermal denaturation of hexokinase was retarded in the presence of one of
its substrates.
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