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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
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.
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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