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1) You are studying an enzyme that catalyzes the following reaction, where k₂ is the rate-limiting step: E+SES > E + P You obtain kinetic data for a wild type enzyme and a mutant. The two enzymes differ by one amino acid position in the protein. From the data, you calculate the following parameters. Wild type Mutant Maximum Velocity 100 μM/min 1 μM/min Км 10 mM 0.1 mM a) Describe the effects of the mutation on both substrate binding and catalysis. Rationalize the effect of the mutation using an energy landscape diagram. b) What is the initial velocity of the reaction catalyzed by the wild type enzyme at a substrate concentration of 10 mM? At a substrate concentration of 4.8 mM? c) Which enzyme will produce more product at equilibrium?

1) You are studying an enzyme that catalyzes the following reaction, where k₂ is the rate-limiting step: E+SES > E + P You obtain kinetic data for a wild type enzyme and a mutant. The two enzymes differ by one amino acid position in the protein. From the data, you calculate the following parameters. Wild type Mutant Maximum Velocity 100 μM/min 1 μM/min Км 10 mM 0.1 mM a) Describe the effects of the mutation on both substrate binding and catalysis. Rationalize the effect of the mutation using an energy landscape diagram. b) What is the initial velocity of the reaction catalyzed by the wild type enzyme at a substrate concentration of 10 mM? At a substrate concentration of 4.8 mM? c) Which enzyme will produce more product at equilibrium?

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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1) You are studying an enzyme that catalyzes the following reaction, where k₂ is the rate-limiting step: E+SES > E + P You obtain kinetic data for a wild type enzyme and a mutant. The two enzymes differ by one amino acid position in the protein. From the data, you calculate the following parameters. Wild type Mutant Maximum Velocity 100 μM/min 1 μM/min Км 10 mM 0.1 mM a) Describe the effects of the mutation on both substrate binding and catalysis. Rationalize the effect of the mutation using an energy landscape diagram. b) What is the initial velocity of the reaction catalyzed by the wild type enzyme at a substrate concentration of 10 mM? At a substrate concentration of 4.8 mM? c) Which enzyme will produce more product at equilibrium?
Transcribed Image Text:1) You are studying an enzyme that catalyzes the following reaction, where k₂ is the rate-limiting step: E+SES > E + P You obtain kinetic data for a wild type enzyme and a mutant. The two enzymes differ by one amino acid position in the protein. From the data, you calculate the following parameters. Wild type Mutant Maximum Velocity 100 μM/min 1 μM/min Км 10 mM 0.1 mM a) Describe the effects of the mutation on both substrate binding and catalysis. Rationalize the effect of the mutation using an energy landscape diagram. b) What is the initial velocity of the reaction catalyzed by the wild type enzyme at a substrate concentration of 10 mM? At a substrate concentration of 4.8 mM? c) Which enzyme will produce more product at equilibrium?
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