What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate? **Fig. 10: Michaelis-Menten Plot using a value of 0.01 mM for Km.**Notice:1) That a new set of calculated values in column C has been generated.2) That by using these new data, a new best-fit Michaelis-Menten plot (red curve) has been generated.Fig. 10 shows that the rates for the new enzyme-catalyzed reaction (red curve) were higher than those originally obtained (blue symbols).**Detailed Explanation of Graphs and Diagrams:**- **Table:** - This includes columns labeled [S] (substrate concentration in mM), V0 (initial velocity), Km, and Vmax, with specific numerical values provided for each parameter. The new values for V0 are listed in column C. - **Graph:** - The bottom axes represent substrate concentration, and the vertical axes display reaction rate. - The graph contains a red curve and blue symbols. The red curve represents the new Michaelis-Menten fit calculated with the new values, while the blue symbols represent previously obtained data points.The visual illustrates the comparison between calculated values and initially obtained data, highlighting differences in enzyme activity based on altered parameters.

The value of KM is inversely related to the affinity of the enzyme for its substrate. High values of…

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Biochemistry

What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate?

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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