Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 8, Problem 6P
Interpretation Introduction
Interpretation:
The fundamental mechanism by which enzymes enhances the rate of
Concept introduction:
Enzymes being a catalyst enhances the
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For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s.
a)
Calculate the Ks and KM for this reaction.
b)
Does substrate binding achieve equilibrium or steady state?
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?
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If the initial Et concentration is 0.25mM, what is Vmax?
An enzyme lowers the activation energy, (AG) of a reaction from 50.0 kcal/mol to 40.0
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Chapter 8 Solutions
Biochemistry
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
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