Assume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter25: Nitrogen Acquisition And Amino Acid Metabolism
Section: Chapter Questions
Problem 22P
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Assume that an enzyme-catalyzed reaction follows the scheme shown:
E+S SES
→E + P
k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s
What is the dissociation constant for the enzyme-substrate, K,?
What is the Michaelis constant, Km, for this enzyme?
What is the turnover number, Keat, for this enzyme?
What is the catalytic efficiency for the enzyme?
If the initial Et concentration is 0.25mM, what is Vmax?
Transcribed Image Text:Assume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?
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