For a Michaelis-Menten reaction, k₁=5 x 107/M-s, k-1-2 x 104/s, and k2=4 x 10²/s.Calculate the Ks and KM for this reaction.Does substrate binding achieve equilibrium or steady state?

According to enzyme kinetics k1 is the formation of the ES complex,k-1 is the rate of dissociation…

Answered: For a Michaelis-Menten reaction, k₁=5 x…

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

Problem 1P

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For a Michaelis-Menten reaction, k₁=5 x 107/M-s, k-1-2 x 104/s, and k2=4 x 102/ Calculate the Ks and KM for this reaction. Does substrate binding achieve equilibrium or steady state?