### Understanding the Michaelis Constant (KM)In the study of enzyme kinetics, the Michaelis constant (KM) for a substrate is a crucial parameter that defines the substrate concentration at which the reaction rate is at half of its maximum. This concept can be expressed in a few different ways:a. **k-1/k2**: This option suggests a relation involving reaction rate constants. Typically, KM is more directly related to the breakdown and formation of enzyme-substrate complexes rather than a simple ratio of these constants.b. **Vmax/2**: This option is incorrect as KM specifically refers to substrate concentration, not the velocity directly.c. **[S] at Vmax/2**: This is the correct representation. KM is defined as the substrate concentration ([S]) at which the reaction velocity is half of Vmax (maximum velocity).Understanding KM helps in determining the affinity of an enzyme for its substrate; a lower KM indicates a higher affinity, meaning less substrate is needed to reach half of the maximum reaction rate.

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Answered: The KM for a substrate is equal to a.…

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The KM for a substrate is equal to a. k-1/k2. b. Vmax/2. c. [S] at Vmax/2.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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