An enzyme that follows Michaelis-Menten kinetics has a KM value of 16.0 uM and a kcat value of 181 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures
An enzyme that follows Michaelis-Menten kinetics has a KM value of 16.0 uM and a kcat value of 181 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures
Principles of Instrumental Analysis
7th Edition
ISBN:9781305577213
Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Chapter30: Capillary Electrophoresis, Electrochromatography, And Field-flow Fractionation
Section: Chapter Questions
Problem 30.9QAP
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A An enzyme that follows Michaelis-Menten kinetics has a KM value of 16.0 uM and a kcat value of 181 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures
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