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Which of the following assumptions or limitations are required to derive the Michaelis-Menten rate equation? Question 18 options: The concentration of enzyme is in excess over the concentration of substrate to ensure pseudo-first order conditions where the concentration of enzyme can be considered not to change during the course of the reaction

Which of the following assumptions or limitations are required to derive the Michaelis-Menten rate equation? Question 18 options: The concentration of enzyme is in excess over the concentration of substrate to ensure pseudo-first order conditions where the concentration of enzyme can be considered not to change during the course of the reaction

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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Which of the following assumptions or limitations are required to derive the Michaelis-Menten rate equation? Question 18 options: The concentration of enzyme is in excess over the concentration of substrate to ensure pseudo-first order conditions where the concentration of enzyme can be considered not to change during the course of the reaction A "steady-state condition" exists in which the rate of the forward reaction going from substrate to product equals the rate of the backward reaction going from product to substrate The rate of the enzyme catalyzed reaction is only being measured at the start of the reaction before an appreciable amount of product accumulates The concentration of substrate added to the reaction is assumed not to change appreciably during the time course of the experiment used to measure the rate of reaction. please note that this question is multi-select
Transcribed Image Text:Which of the following assumptions or limitations are required to derive the Michaelis-Menten rate equation? Question 18 options: The concentration of enzyme is in excess over the concentration of substrate to ensure pseudo-first order conditions where the concentration of enzyme can be considered not to change during the course of the reaction A "steady-state condition" exists in which the rate of the forward reaction going from substrate to product equals the rate of the backward reaction going from product to substrate The rate of the enzyme catalyzed reaction is only being measured at the start of the reaction before an appreciable amount of product accumulates The concentration of substrate added to the reaction is assumed not to change appreciably during the time course of the experiment used to measure the rate of reaction. please note that this question is multi-select
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